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100  * Licensed under the MIT license - http://opensource.org/licenses/MIT
101  * Copyright (c) 2015 Daniel Eden
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222<div class="et_pb_section_0 et_pb_section et_section_regular et_block_section"><div class="et_pb_row_0 et_pb_row et_block_row"><div class="et_pb_column_0 et_pb_column et_pb_column_4_4 et-last-child et_block_column et_pb_css_mix_blend_mode_passthrough"><div class="et_pb_image_0 et_pb_image et_pb_module et_block_module"><span class="et_pb_image_wrap"><img fetchpriority="high" decoding="async" src="https://snelllab.website/wp-content/uploads/2019/03/hwi-headers__0004_header5.jpg" width="1500" height="118" srcset="https://snelllab.website/wp-content/uploads/2019/03/hwi-headers__0004_header5.jpg 1500w, https://snelllab.website/wp-content/uploads/2019/03/hwi-headers__0004_header5-300x24.jpg 300w, https://snelllab.website/wp-content/uploads/2019/03/hwi-headers__0004_header5-1024x81.jpg 1024w, https://snelllab.website/wp-content/uploads/2019/03/hwi-headers__0004_header5-768x60.jpg 768w" sizes="(max-width: 1500px) 100v
222w, 1500px" class="wp-image-7288" title="hwi-headers__0004_header5" /></span></div></div></div><div class="et_pb_row_1 et_pb_row et_block_row"><div class="et_pb_column_1 et_pb_column et_pb_column_4_4 et-last-child et_block_column et_pb_css_mix_blend_mode_passthrough"><div class="et_pb_text_0 et_pb_text et_pb_bg_layout_light et_pb_module et_block_module"><div class="et_pb_text_inner"><h1>Laboratory News</h1>
223</div></div></div></div><div class="et_pb_row_2 et_pb_row et_block_row"><div class="et_pb_column_2 et_pb_column et_pb_column_4_4 et-last-child et_block_column et_pb_css_mix_blend_mode_passthrough"><div class="et_pb_module et_d4_element dica_divi_carousel dica_divi_carousel_0">
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241					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/20-years-of-crystals-2022.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_0">
242									
243									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/20-years-of-crystals-2022.pdf" target="_blank">20 Years of Crystal Hits</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/actacryst_D_20years-230x300.png" width="230" height="300" alt="" class="wp-image-25452 alignnone size-medium" /></p>
244<p><span>Diffraction-based structural methods contribute a large fraction of the biomolecular structural models available, providing a critical understanding of macromolecular architecture. These methods require crystallization of the target molecule, which remains a primary bottleneck in crystal-based structure determination. The National High-Throughput Crystallization Center at Hauptman–Woodward Medical Research Institute has focused on overcoming obstacles to crystallization through a combination of robotics-enabled high-throughput screening and advanced imaging to increase the success of finding crystallization conditions. This paper will describe the lessons learned from over 20 years of operation of our high-throughput crystallization services. The current experimental pipelines, instrumentation, imaging capabilities and software for image viewing and crystal scoring are detailed. New developments in the field and opportunities for further improvements in biomolecular crystallization are reflected on.</span></p></div>     </div>
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255					 <div class="dica-item image_top" data-link="https://www.iucr.org/iucr/governance/advisory-committees/book-series" data-target="_blank" data-hash="dica_divi_carouselitem_1">
256									
257									<div class="dica-item-content"><h4 class="item-title"><a href="https://www.iucr.org/iucr/governance/advisory-committees/book-series" target="_blank" rel="noopener">Appointment to International Book Committee</a></h4> <h6 class="item-subtitle">News</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/snell_head-300x300.jpg" width="300" height="300" alt="" class="wp-image-25450 alignnone size-medium" /></p>
258<p>Dr. Snell was appointed to the International Union of Crystallography (IUCr) Committee as a member of the Book Series Committee. The Committee recommends new book publications to the IUCr Executive Committee and the Delegates of Oxford University Press. Recommended publications are IUCr monographs, which are in-depth expositions of specialized topics in crystallography, crystallography texts providing standardized methods and approaches, and related books.</p></div>
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269					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/pulavarti-et-al-2022-from-protein-design-to-the-energy-landscape-of-a-cold-unfolding-protein.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_2">
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271									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/pulavarti-et-al-2022-from-protein-design-to-the-energy-landscape-of-a-cold-unfolding-protein.pdf" target="_blank">Landscape of a Cold Unfolding Protein</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/cold_fold-300x201.jpg" width="300" height="201" alt="" class="wp-image-25453 alignnone size-medium" srcset="https://snelllab.website/wp-content/uploads/2024/06/cold_fold-300x201.jpg 300w, https://snelllab.website/wp-content/uploads/2024/06/cold_fold.jpg 435w" sizes="(max-width: 300px) 100vw, 300px" /></p>
272<p><span>Understanding protein folding is crucial for protein sciences.  We created the cold unfolding 4-helix bundle DCUB1 with a de novo designed bipartite hydrophilic/hydrophobic core featuring a hydrogen bond network which extends across the bundle in order to study the relative importance of hydrophobic versus hydrophilic protein–water interactions for cold unfolding. Structural and thermodynamic characterization resulted in the discovery of a complex energy landscape for cold transitions, while the heat unfolded state is a random coil.  Our results suggest that cold unfolding is initiated by the intrusion of water into the hydrophilic core network and that cooperativity can be tuned by varying the number of core hydrogen bond networks. Protein design has proven to be invaluable to explore the energy landscapes of cold states and to robustly test related theories.</span></p></div>     </div>
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283					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/SARS-CoV-2-near-physiological-2021.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_3">
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285									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/SARS-CoV-2-near-physiological-2021.pdf">COVID-19 Research</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/covid-300x300.jpg" width="300" height="300" alt="" class="wp-image-25454 alignnone size-medium" /></p>
286<p><span>The COVID-19 pandemic has resulted in 198 million reported infections and more than 4 million deaths as of July 2021</span><span>. </span><span> To assist in drug repurposing and design, we determined two apo structures of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease at ambient temperature by serial femtosecond X-ray crystallography. We employ detailed molecular simulations of selected known main protease inhibitors with the structures and compare binding modes and energies. The combined structural and molecular modeling studies not only reveal the dynamics of small molecules targeting the main protease but also provide invaluable opportunities for drug repurposing and structure-based drug design strategies against SARS-CoV-2.</span></p></div>     </div>
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297					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/saxs-scavengers-2021.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_4">
298									
299									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/saxs-scavengers-2021.pdf">SAXS studies of radical scavengers</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/JSR_2021_09_cover--230x300.jpg" width="230" height="300" alt="" class="wp-image-25448 alignnone size-medium" /></p>
300<p><span>X-ray-based techniques are a powerful tool in structural biology but the radiation-induced chemistry that results can be detrimental and may mask an accurate structural understanding.  Using a protein designed to undergo a large-scale structural change from breakage of a di­sulfide bond, radiation damage can be monitored with small-angle X-ray scattering. We have quantitatively evaluated how three scavengers commonly used in crystallographic experiments – sodium nitrate, cysteine, and ascorbic acid – perform in solution at 10°C. </span><span> The SAXS-based method can detect damage at X-ray doses far lower than those accessible crystallographically, thereby providing a detailed picture of scavenger processes. Our engineered approach might provide a platform for more systematic and comprehensive screening of radioprotectants that can directly inform mitigation strategies for both solution and crystallographic experiments, while also clarifying fundamental radiation damage mechanisms and allowing the study of low dose radiation.</span></p></div>
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313									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/SAXS-disulfide-2020.pdf" target="_blank">Engineering High-Resolution Insight</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/dimer-300x212.jpg" width="300" height="212" alt="" class="wp-image-25455 alignnone size-medium" /></p>
314<p><span>Radition chemistry in biological X-ray crystallography iproduces both global and site-specific damage. Site specific damage can misdirect the biological interpretation of the structural models produced.  The doses used for X-ray crystallography are typically in the kilo-gray to mega-gray range. While disulfide bonds are among the most significantly affected species in proteins in the crystalline state at both cryogenic and higher temperatures, there is limited information on their response to low X-ray doses in solution, the details of which might inform biomedical applications of X-rays. An engineered a protein  approach enables small angle X-ray scattering (SAXS), to detect and monitor a residue specific process. The ability to generate a large-scale change through a site-specific interaction represents a promising tool for advancing radiation damage studies under solution conditions and in dose regimes of health-related impact.</span></p></div>     </div>
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325					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/COVID-structura-biology-2021.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_6">
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327									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/COVID-structura-biology-2021.pdf" target="_blank">Structural Biology Fighting COVID-19</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/Fig1_nsp6-300x173.png" width="300" height="173" alt="" class="wp-image-25456 alignnone size-medium" /></p>
328<p><span>The global COVID-19 pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) wreaked unprecedented havoc on global society. Yet the sheer magnitude and uniqueness of this event has also spawned a massive mobilization of effort in the scientific community to investigate the virus, to develop therapeutics and vaccines, and to understand the public health impacts. Structural biology has been at the center of these efforts, and we reflect on the status of structural science vis-a`-vis its role in the fight against COVID-19, to register the unprecedented response and to contemplate the role of structural biology in addressing future outbreak threats.  Examining SARS-CoV-2 protein structures that have been deposited in the PDB since the virus was first identified allows a unique window into the power of structural biology and a snapshot of the advantages of the different techniques available, as well as insight into the complementarity of the structural methods</span></p></div>     </div>
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341									<div class="dica-item-content"><h4 class="item-title">Elected to ACA Fellow</h4> <h6 class="item-subtitle">News</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/Snell2_final-300x300.jpg" width="300" height="300" alt="" class="wp-image-25531 alignnone size-medium" /></p>
342<p>Dr. Edward Snell was elected as American Crystallographic Association Fellow. The American Crystallographic Association – the Structural Science Society – established the Fellows distinction to recognize a high level of excellence in scientific research, teaching, and professional duties, but also service, leadership, and personal engagement in the world of crystallography and science.</p></div>
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353					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/microgravity_2021.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_8">
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355									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/microgravity_2021.pdf" target="_blank">Crystallization in Space</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/iss-300x176.jpg" width="300" height="176" alt="" class="wp-image-25447 size-medium" /></p>
356<p><span>More regular space flight is becoming a reality, new diffraction data detectors have become available that have both a faster readout and lower noise, a new generation of extremely bright X-ray sources and X-ray free-electron lasers (XFELs) have become available with beam collimation properties well suited geometrically to more perfect protein crystals. Neutron sources, instrumentation, and methods have also advanced greatly for yielding complete structures at room temperature and radiation damage-free. The larger volumes of protein crystals from microgravity can synergise well with these recent neutron developments. Unfortunately, progress in harnessing these new technologies to maximize the benefits seen in microgravity-grown crystals has been patchy and even disappointing. Despite detailed theoretical analysis and key empirical studies, crystallization in microgravity has not yet produced the results that demonstrate its potential. In this review we present some of the key lessons learned and show how processes could yet be optimized given these new developments</span></p></div>     </div>
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367					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/networks-across-scale-2021.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_9">
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369									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/networks-across-scale-2021.pdf" target="_blank">Networks Across Scales</a></h4> <h6 class="item-subtitle">Science</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/Network-300x270.png" width="300" height="270" alt="" class="wp-image-25449 alignnone size-medium" /></p>
370<p><span>A wide range of networks exist in biology, from gene regulatory networks important for organismal development, protein interaction networks that govern physiology and metabolism, and neural networks that store and convey information to networks of microbes that form microbiomes within hosts, animal contact networks that underlie social systems, and networks of populations on the landscape connected by migration. Increasing availability of extensive (big) data is amplifying our ability to quantify biological networks. Similarly, theoretical methods that describe network structure and dynamics are being developed. In this paper, we explore the opportunity for discovering universal laws connecting the structure of biological networks with their function, positioning them on the spectrum of time-evolving network structure, that is, dynamics of networks, from highly stable to exquisitely sensitive to perturbation. If such general laws exist, they could transform our ability to predict the response of biological systems to perturbations—an increasingly urgent priority in the face of anthropogenic changes to the environment that affect life across the gamut of organizational scales.</span></p></div>     </div>
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379			</div><div class="et_pb_text_1 et_pb_text et_pb_bg_layout_light et_pb_module et_block_module"><div class="et_pb_text_inner"><h2><strong>Structures involving the laboratory</strong></h2>
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398					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/Taberman_et_al_2019.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_10">
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400									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/Taberman_et_al_2019.pdf" target="_blank">X-ray radiation study on xylose isomerase</a></h4> <h6 class="item-subtitle">6QRY</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/6qry-e1717823977565-300x238.png" width="300" height="238" alt="" class="wp-image-25470 alignnone size-medium" /></p>
401<p><span>A radiation chemistry study on the impacr of dose on structural information using xylose isomerase as an example. The results show that information interpreted as mechanism can be a result of the X-rays used to produce the models. See also PDB entries 6QRX, 6QRW, 6QRV, 6QRU, 6QRT, 6QRS, 6QRR.</span></p></div>     </div>
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412					 <div class="dica-item image_top" data-link="https://www.iucr.org/iucr/governance/advisory-committees/book-series" data-target="_blank" data-hash="dica_divi_carouselitem_11">
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414									<div class="dica-item-content"><h4 class="item-title"><a href="https://www.iucr.org/iucr/governance/advisory-committees/book-series" target="_blank" rel="noopener">Latency Associated Peptide unbound to TGF-β1</a></h4> <h6 class="item-subtitle">6P7J</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/6p7j-e1717824358507-300x257.png" width="300" height="257" alt="" class="wp-image-25472 alignnone size-medium" /></p>
415<p>A study on the dissociation of the inhibitory protein latency associated peptide (LAP) from transforming growth factor β1, important for those undergoing radiation therapy.</p></div>     </div>
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419				
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426					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/grime-et-al-2019-high-throughput-pixe-as-an-essential-quantitative-assay-for-accurate-metalloprotein-structural-2020.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_12">
427									
428									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/grime-et-al-2019-high-throughput-pixe-as-an-essential-quantitative-assay-for-accurate-metalloprotein-stru
428ctural-2020.pdf" target="_blank">The C-terminal domain (277-440) of a putative chitobiase from Bacteroides thetaiotaomicron.</a></h4> <h6 class="item-subtitle">6OE2</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/6OE2-e1717827704467-300x245.png" width="300" height="245" alt="" class="wp-image-25475 alignnone size-medium" /></p>
429<p><span>PIXE data revealed Mn as the experimentally determined metal rather than Zn as originally modeled. This changed the coordination number of the metal from 4 to 5. This may have an importance in understanding the basics of Tay-Sachs and Sandhoff disease.</span></p></div>     </div>
430							</div>
431				</div>
432			</div><div class="et_pb_module et_d4_element dica_divi_carouselitem dica_divi_carouselitem_13 et_clickable">
433				
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440					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/grime-et-al-2019-high-throughput-pixe-as-an-essential-quantitative-assay-for-accurate-metalloprotein-structural-2020.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_13">
441									
442									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/grime-et-al-2019-high-throughput-pixe-as-an-essential-quantitative-assay-for-accurate-metalloprotein-structural-2020.pdf">The nucleotide-binding protein AF_226 in complex with ADP from Archaeoglobus fulgidus</a></h4> <h6 class="item-subtitle">6OBY</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/6oby-e1717825321992-300x223.png" width="300" height="223" alt="" class="wp-image-25477 alignnone size-medium" /></p>
443<p>Nucleotide binding proteins play a crucial role in many diseases. In this case PIXE identified Co bound rather than the modeled Zn. It is not known if the Co was promisciously bound and if it is biologically relevant.</p></div>     </div>
444							</div>
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447				
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454					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/grime-et-al-2019-high-throughput-pixe-as-an-essential-quantitative-assay-for-accurate-metalloprotein-structural-2020.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_14">
455									
456									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/grime-et-al-2019-high-throughput-pixe-as-an-essential-quantitative-assay-for-accurate-metalloprotein-structural-2020.pdf">A putative histidinol phosphatase hisK from Listeria monocytogenes</a></h4> <h6 class="item-subtitle">6NLR</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/6nlr-e1717825635802-300x216.png" width="300" height="216" alt="" class="wp-image-25478 alignnone size-medium" /></p>
457<p>PIXE combined with tha anomalous X-ray signal allowed the metals in the tri-nuclear metal center to be correctly identified replacing the Fe and Zn with Fe, Co, and Mn. A sulfate ion was revealed in the active site agreeing well with literature on related proteins.</p></div>     </div>
458							</div>
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461				
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468					 <div class="dica-item image_top"   data-hash="dica_divi_carouselitem_15">
469									
470									<div class="dica-item-content"><h4 class="item-title">Wild type T4 lysozyme structure</h4> <h6 class="item-subtitle">4SOW</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/4s0w-e1717825958623-300x256.png" width="300" height="256" alt="" class="wp-image-25481 alignnone size-medium" /></p>
471<p><span>Part of a study aimed at deliberatly de-crystallizing T4 lysozyme using surface mutations to understand the influence of different chemistries on the crystallization process.</span></p></div>
471     </div>
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475				
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482					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/disulphide-radiation-2013.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_16">
483									
484									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/disulphide-radiation-2013.pdf" target="_blank">Understanding the radiation chemistry around disulfide bond breakage </a></h4> <h6 class="item-subtitle">4H9I</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/4H9I-e1717826139140-300x214.png" width="300" height="214" alt="" class="wp-image-25482 alignnone size-medium" /></p>
485<p><span>Disulfide bond damage is seen in X-ray structures but is also caused by free radical production in the body and drives key biological mechanisms. This study used lysozyme to study this process. Related models are 4H9E, 4H9C, 4H9B, 4H9A, 4H94, 4H93, 4H8Z, 4H8Y, and 4H8X.</span></p></div>     </div>
486							</div>
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489				
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496					 <div class="dica-item image_top" data-link="https://snelllab.website/wp-content/uploads/2024/06/pand_panz-2015.pdf" data-target="_blank" data-hash="dica_divi_carouselitem_17">
497									
498									<div class="dica-item-content"><h4 class="item-title"><a href="https://snelllab.website/wp-content/uploads/2024/06/pand_panz-2015.pdf" target="_blank">The Structure of the Pand/Panz Protein Complex</a></h4> <h6 class="item-subtitle">4CS0</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/4cs0-e1717826421255-300x164.png" width="300" height="164" alt="" class="wp-image-25483 alignnone size-medium" /></p>
499<p>In this study our collaborators determined the structure and we used SAXS to model the protein complex. The information provides a mechanistic understanding of regulation in the body. See also PDB entries 4CRZ and 4CRY.</p></div>     </div>
500							</div>
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510					 <div class="dica-item image_top"  data-target="_blank" data-hash="dica_divi_carouselitem_18">
511									
512									<div class="dica-item-content"><h4 class="item-title">The tRNA Binding Domain of Glutaminyl-tRNA Synthetase from Saccharomyces cerevisiae</h4> <h6 class="item-subtitle">3TL4</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/3tl4-e1717827179530-300x190.png" width="300" height="190" alt="" class="wp-image-25488 alignnone size-medium" /></p>
513<p><span>Eukaryotic glutaminyl-tRNA synthetase (GlnRS) contains an appended N-terminal domain (NTD) whose precise function is unknown. The structure of  an N-terminal domain enabled a model of the full-length enzyme in solution, and modeling its binding to tRNA suggesting that in eukaryotes there is motion of the C-terminal domain through conserved hinge. The domain is nearly ubiquitious among eukaryotic GlnRS species but lacking in prokaryotic holologs.</span></p></div>     </div>
514							</div>
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517				
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524					 <div class="dica-item image_top"  data-target="_blank" data-hash="dica_divi_carouselitem_19">
525									
526									<div class="dica-item-content"><h4 class="item-title">Glutaminyl-tRNA Synthetase from Saccharomyces Cerevisiae</h4> <h6 class="item-subtitle">4H3S</h6>  <div class="content"><p><img loading="lazy" decoding="async" src="https://snelllab.website/wp-content/uploads/2024/06/4h3s-e1717827637164-300x161.png" width="300" height="161" alt="" class="wp-image-25489 alignnone size-medium" /></p>
527<p><span>In all organisms, aminoacyl tRNA synthetases covalently attach amino acids to their cognate tRNAs. Many eukaryotic tRNA synthetases have acquired appended domains, whose origin, structure and function are poorly understood. The N-terminal appended domain (NTD) of glutaminyl-tRNA synthetase (GlnRS) is intriguing since GlnRS is primarily a eukaryotic enzyme, whereas in other kingdoms Gln-tRNAGln is primarily synthesized by first forming Glu-tRNAGln, followed by conversion to Gln-tRNAGln by a tRNA-dependent amidotransferase. . Our results suggest a possible origin and function of the NTD that would link the phylogenetically diverse mechanisms of Gln-tRNAGln synthesis.</span></p></div>
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554<div class="et_pb_text_0_tb_footer et_pb_text et_pb_bg_layout_light et_pb_module et_block_module"><div class="et_pb_text_inner"><p><strong>Education</strong></p>
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556<li>John Moores University of Liverpool, UK, Physics, B.Sc. Hons (1st) – 1992.</li>
557<li>University of Manchester, UK, Chemistry, Ph.D. – 1996.</li>
558<li>NASA Biophysics Laboratory, Marshall Space Flight Center, USA, National Research Council Fellow - 1996 - 1999.</li>
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564<div class="et_pb_text_1_tb_footer et_pb_text et_pb_bg_layout_light et_pb_module et_block_module"><div class="et_pb_text_inner"><p><strong>Contact</strong><br />Edward Snell, PhD<br />T: 716-881-7573<br />[email protected]<br /><a href="https://snelllab.website">snelllab.website</a></p>
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626<script id="divi-script-library-frontend-scripts-js-extra">
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628var et_frontend_scripts = {"builderCssContainerPrefix":"#et-boc","builderCssLayoutPrefix":"#et-boc .et-l"};
629var et_builder_utils_params = {"condition":{"diviTheme":true,"extraTheme":false},"scrollLocations":["app","top"],"builderScrollLocations":{"desktop":"app","tablet":"app","phone":"app"},"onloadScrollLocation":"app","builderType":"fe"};
630var et_pb_box_shadow_elements = [];
631//# sourceURL=divi-script-library-frontend-scripts-js-extra
632</script>
vendor: 1 bytes, line 632
632
633<script id="divi-script-library-frontend-scripts-js" src="https://snelllab.website/wp-content/themes/Divi/includes/builder-5/visual-builder/build/script-library-frontend-scripts.js?ver=5.13.1"></script>
vendor: 1 bytes, line 633
633
634<script id="divi-carousel-frontend-bundle-js" src="https://snelllab.website/wp-content/plugins/dg-divi-carousel/scripts/frontend-bundle.min.js?ver=2.0.26"></script>
vendor: 1 bytes, line 634
634
635<script id="carousel-layouts-frontend-bundle-js" src="https://snelllab.website/wp-content/plugins/divi-carousel-maker/scripts/frontend-bundle.min.js?ver=2.1.20"></script>
vendor: 1 bytes, line 635
635
636<script id="divi-script-library-multi-view-js-extra">
637var diviBreakpointData = {"enabledBreakpoints":[{"order":50,"baseDevice":true,"enable":true,"name":"desktop"},{"order":30,"enable":true,"maxWidth":{"value":"980px","default":980},"name":"tablet"},{"order":10,"enable":true,"maxWidth":{"value":"767px","default":767},"name":"phone"}],"enabledBreakpointNames":["desktop","tablet","phone"],"baseBreakpointName":"desktop"};
638//# sourceURL=divi-script-library-multi-view-js-extra
639</script>
vendor: 1 bytes, line 639
639
640<script id="divi-script-library-multi-view-js" src="https://snelllab.website/wp-content/themes/Divi/includes/builder-5/visual-builder/build/script-library-multi-view.js?ver=5.13.1"></script>
640
641	
642			<span class="et_pb_scroll_top et-pb-icon"></span>
643	</body>
644</html>
645
646
647<!-- Page cached by LiteSpeed Cache 7.9.1 on 2026-10-05 01:37:15 -->

Line numbers count LF bytes from the start of the resource, as the search results do. Vendor segments are library code the classifier recognised; they are stored but not indexed. Bytes are shown as Latin1 characters, one per byte.