The Snell Laboratory
Dr. Edward Snell is a biophysicist who leads the Hauptman-Woodward Medical Research Institute. He has almost 80 publications, four book chapters, and two books. He and serves on numerous advisory committees. The Snell Group is engaged in methods development that leads to a deeper understanding of biological structure, function, and mechanism. The laboratory is predominantly interested in crystallography with an ever-increasing focus on complementary techniques to extend and enhance the understanding of dynamics on top of the structure. Ongoing projects include the enhancement of high-throughput crystallization processes, accurate interpretation of metalloprotein structure, and specific structural projects related to cancer therapy and treatment. Dr. Snell is also the Director of the NSF BioXFEL Science and Technology Center, an effort to develop the biological applications of X-ray Free Electron Lasers.
The COVID-19 pandemic has impacted almost every aspect of our lives in the past year and continues to do so. In March, at the one-year mark of the World Health Organization declaration that COVID-19 is a pandemic, researchers at HWI – Drs. Miranda Lynch, Edward Snell and Sarah Bowman – delved into...
A significant problem in biological X-ray crystallography is the radiation chemistry caused by the incident X-ray beam. This produces both global and site-specific damage. Site-specific damage can misdirect the biological interpretation of the structural models produced. Cryo-cooling crystals have...
Dr. Timothy Stachowski, defended his Ph.D. thesis entitled "Towards Understanding the Structural Impact from Therapeutic Radiation Doses from Mechanisms in Engineered Systems to to TGF-β1". Dr. Stachowski was a Biophysics Ph.D. student in the Snell Laboratory through the Roswell Park Comprehensive...
Transforming growth factor -1 (TGF-1) is a secreted signaling protein that directs many cellular processes and is an attractive target for the treatment of several diseases. This study looks at the regulatory mechanism of TGF-1 and is of fundamental importance for therapeutic development. The...
Metalloproteins play a key role in the progression of many diseases. Using ion beam analysis through particle-induced X-ray emission (PIXE) and anomalous X-ray analysis we have quantitatively identified the metal atoms in 30 previously structurally characterized proteins using minimal sample...
Xylose isomerase (XI) is an industrially important metalloprotein studied for decades. Its reaction mechanism has been postulated to involve the movement of the catalytic metal cofactor to several different conformations. Here, a dose-dependent approach was used to investigate the radiation damage...
Dissociation of transforming growth factor beta-1 (TGF-β1) from the inhibitory protein latency-associated peptide (LAP) can occur from low doses of X-ray irradiation of the LAP–TGF-β1 complex, resulting in the activation of TGF-β1 and can have health-related consequences. Using the tools and...
A book entitled Biological Small Angle Scattering: Theory and Practice, by Eaton Lattman, Thomas Grant, and Edward Snell, is part of an International Union of Crystallography series that provides in-depth knowledge of specialized topics. The technique of small-angle solution scattering has been...
Some of the structures the laboratory has been involved with
Research in the Snell Laboatory
Our current research focus is in the study of the structural impacts of X-ray radiation at therapeutic doses and understanding a range of biological systems that are involved in free-radical based biological processes. This is reflected in a number of our recent publications developing a sensitive measure of residue-specific radiation chemistry at doses of a few Grey, looking at the dynamics of systems thought to be triggered by free radical driven processes, and the accurate metal determination in metalloproteins. All provide the tools and techniques for the study of medically important systems that are linked to free radical processes.
Our research builds on a history of developments in crystallization, the use of SAXS, precious radiation chemistry studies, and methods to optimize and make use of the physical quality of protein crystals. We are extending our expertise to cryo-electron microscopy and spectroscopic methods. Publications related to our current and historical focus areas are provided at the bottom of the page.
We have developed methods to make high-throughput become high-output. We have aimed to decrease the steps involved in going from an initial crystallization hit to a diffraction pattern through several developments. The first of these is in defining a means to optimize crystallization conditions using only the chemicals causing the initial hit. A simple drop volume ratio coupled with temperature variation allows the closet space to the nucleation and metastable region in the phase diagram to be traversed. If there is not enough sample to replicate or optimize a hit a novel means to reproducibly extract and mount the crystal as devised. Very simply, using the transparent properties of the plate observation could occur opposite to the extraction. A capillary can remove the crystal and deposit it into a loop. In situ methods have superseded this approach but they will be a topic of a later citation. Historically we can learn a lot, successful approaches in the past will be successful in the future. Coupling this with the knowledge that many crystals appear before we can observe them microscopically and the methods that we can use to observe them at these stages is useful knowledge in exploring and understanding fundamental crystal growth. These developments are made available to the community from our screening laboratory.
Development and use of SAXS
We have made use of complementary techniques to explain the difference between tRNA synthesis in prokaryotes and eukaryotes. Small-angle X-ray scattering (SAXS) resolution was poor and the results ambiguous. With the advent of modern detectors, improved beams, and the computational power to run mathematically intense algorithms SAXS has changed. The combination of SAXS, crystallography, and molecular dynamics was used to explain the differences in eukaryotic and prokaryotic tRNA synthesis, specifically the role of appended domains in eukaryotic systems. In doing so we have established the fidelity of SAXS as a technique and developed high-throughput methods to characterize a sample and determine if there are different oligomeric states in solution and crystal. In doing so we established quality criteria for SAXS data that distinguishes between data that can be treated routinely by standard software from that needing an expert analysis and finally data that is not usable. This opens up a previously subjective analysis for the use of SAXS by a much wider audience and enables its complementary application with other structural techniques.
Radiation chemistry impact on the structure
We developed a physical model of disulfide bond damage from irradiation based on studies on cryocooling and using a combination of crystallography, spectroscopy, and electron paramagnetic resonance. We determined that cryocooling causes a cold wave to flow through the crystal cooling it from the side nearest the cold source to the side furthest from it establishing a gradient across the crystal. Gradients in d-spacing are therefore continuous along the crystal axis. A microbeam would see good data in all points with a gradual increase in cell parameters as a function of distance from the cold source. The beam itself heats the sample. This can be considerable, taking it where OH radicals are immobilized to above this point with detrimental consequences for structural data. Maintaining an air stream to remove heat has a dramatic effect on this process and is a requirement to minimize beam heating even at ambient temperatures. The cooling itself can be reversible using large amounts of cryoprotectants to promote annealing success. Our data shows that disulfide bonds are radicalized in the first image. We discovered an unexpected damage repair process, such that with a sufficient dose rate, the damage that occurs before useful diffraction stops can be reduced.
The physical quality of protein crystals
Probing long-range order in crystallization shows that protein crystals have similar if not better physical characteristics to solid-state crystals. Solid-state physics has used X-ray techniques to characterize crystals for a long time. During the 1990s crystals were being grown in space to use the reduced convection properties of freefall to minimize convection over the crystal surface. Applying rocking width measurements to crystals we found that mosaicity was greatly reduced in a reduced convection growth environment. Unfortunately, mosaicity is a long-range effect while resolution depends on short-range order – diffraction resolution is not enhanced. Topography and reciprocal space mapping confirmed the result and also pointed the way to a means to exploit long-range order for a higher signal to noise, i.e. fine slicing or continuous rotation data collection. This is now possible. Interestingly the physical quality of macromolecular crystals studied at physiological temperatures can be so good that an explicit treatment of diffraction may be needed rather than the kinematical approximation used currently.
Publications by year (click here).
Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing. Durdagi S, Dağ C, Dogan B, Yigin M, Avsar T, Buyukdag C, Erol I, Ertem FB, Calis S, Yildirim G, Orhan MD, Guven O, Aksoydan B, Destan E, Sahin K, Besler SO, Oktay L, Shafiei A, Tolu I, Ayan E, Yuksel B, Peksen AB, Gocenler O, Yucel AD, Can O, Ozabrahamyan S, Olkan A, Erdemoglu E, Aksit F, Tanisali G, Yefanov OM, Barty A, Tolstikova A, Ketawala GK, Botha S, Dao H, Hayes B, Liang M, Seaberg MH, Hunter MS, Batyuk A, Mariani V, Su Z, Poitevin F, Yoon CH, Kupitz C, Sierra RG, Snell EH, and DeMirci H. Structure available online ahead of print.
- Biological networks across scales. Bogdan, P, Caetano-Anolles, Jolles, A, Kim, H, Morris, J, Murphy, C, Royer, Snell EH, Steinbrenner, A. and Strausfeld, N. (2021) Integrative and Comparative Biology in press.
- Structural biology in the time of COVID-19: perspectives on methods and milestones. Lynch, ML, Snell, EH, Bowman, SEJ. (2021) IUCrJ 8, 3, 335-341.
- A SAXS based approach to rationally evaluate radical scavengers – toward eliminating radiation damage in solution and crystallographic studies. Stachowski, TR, Snell, ME, Snell, EH. (2021) Journal of Synchrotron Radiation in press.
- Microgravity as an environment for macromolecular crystallization – an outlook in the era of space stations and commercial space flight. Snell EH and Helliwell JR. (2021) Crystallography Reviews, 8th April, 1-44.
- SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique. Stachowski, T.R., Snell, M.E, and Snell, E.H. PLOS One (2020).
- Structural insights into conformational switching in latency-associated peptide between transforming growth factor β-1 bound and unbound states. Stachowski, T.R., Snell, M.E, & Snell, E.H. IUCrJ 7(2) 238-252 (2020).
- High-Throughput PIXE as an Essential Quantitative Assay for Accurate Metalloprotein Structural Analysis: Development and Application. Grime, G.W., Zeldin, O.B., Snell, M.E., Lowe, E.D., Hunt, J.F., Montelione, G.T., Tong, L., Snell, E.H.* & Garman, E.F* – joint corresponding. JACS (2020) 142, 185-197. doi 10.1021/jacs.9b09186
- Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses, Stachowski, T., Grant, T.D. and Snell, E.H. Journal of Synchrotron radiation in press (2019), 26, 967-979. Doi 10.1107/S1600577519005113.
- Structural knowledge or X-ray damage. A case study on xylose isomerase illustrating both. H, Bury, CS, van der Woerd MJ, Snell EH, Garman EF. J. Synchrotron Radiation. (2019). 26, 931-944.
- Protein and RNA dynamical fingerprinting. Niessen KA, Xu M, George DK, Chen MC, Ferré-D’Amaré AR, Snell EH, Cody V, Pace J, Schmidt M, Markelz AG.Nat Commun. 2019 Mar 4;10(1):1026. doi: 10.1038/s41467-019-08926-3.
- Classification of crystallization outcomes using deep convolutional neural networks. Bruno AE, Charbonneau, P, Newman J, Snell EH, So DR, Vanhoucke V, Watkins CJ, Williams S, Wilson J. PLoS ONE 2018 13(6):e0198883
- Biological Small Angle Scattering Theory and Practice. Lattman, EE., Grant, TD, Snell, EH. Oxford University Press. 2018.
- Double-flow focused liquid injector for efficient serial femtosecond crystallography. Oberthuer D, Knoška J, Wiedorn MO, Beyerlein KR, Bushnell DA, Kovaleva EG, Heymann M, Gumprecht L, Kirian RA, Barty A, Mariani V, Tolstikova A, Adriano L, Awel S, Barthelmess M, Dörner K, Xavier PL, Yefanov O, James DR, Nelson G, Wang D, Calvey G, Chen Y, Schmidt A, Szczepek M, Frielingsdorf S, Lenz O, Snell E, Robinson PJ, Šarler B, Belšak G, Maček M, Wilde F, Aquila A, Boutet S, Liang M, Hunter MS, Scheerer P, Lipscomb JD, Weierstall U, Kornberg RD, Spence JC, Pollack L, Chapman HN, Bajt S. Sci Rep. 2017 Mar 16;7:44628.
- Moving in the Right Direction: Protein Vibrational Steering Function. Niessen KA, Xu M, Paciaroni A, Orecchini A, Snell EH, Markelz AG. Biophys J. 2017;112:933-942.
- The use of haptic interfaces and web services in crystallography: an application for a `screen to beam’ interface. Bruno A, Soares A, Owen R, Snell EH. J. Appl. Cryst. (2016). 49, 2082-2090.
- Computational crystallization. Altan I, Charbonneau P, Snell EH. Arch Biochem Biophys. 2016 Jan 11. pii: S0003-9861(16)30004-2.
- The detection and subsequent volume optimization of biological nanocrystals, Luft JR, Wolfley JR, Franks EC, Lauricella AM, Gualtieri EJ, Snell EH, Xiao R, Everett JK, Montelione GT. Struct Dyn. 2015 May 15;2(4):041710.
- The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A. Monteiro DC, Patel V, Bartlett CP, Nozaki S, Grant TD, Gowdy JA, Thompson GS, Kalverda AP, Snell EH, Niki H, Pearson AR, Webb ME. Chem Biol. 2015 Apr 23;22(4):492-503
- The accurate assessment of small-angle X-ray scattering data. Grant TD, Luft JR, Carter LG, Matsui T, Weiss TM, Martel A, Snell EH. Acta Crystallogr D Biol Crystallogr. 2015 Jan 1;71(Pt 1):45-56.
- A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta. Rossi P, Shi L, Liu G, Barbieri CM, Lee HW, Grant TD, Luft JR, Xiao R, Acton TB, Snell EH, Montelione GT, Baker D, Lange OF, Sgourakis NG. Proteins. 2015 Feb;83(2):309-17.
- Comparing chemistry to outcome: the development of a chemical distance metric, coupled with clustering and hierarchal visualization applied to macromolecular crystallography. Bruno AE, Ruby AM, Luft JR, Grant TD, Seetharaman J, Montelione GT, Hunt JF, Snell EH. PLoS One. 2014 Jun 27;9(6):e100782.
- Identifying, studying and making good use of macromolecular crystals. Calero G, Cohen AE, Luft JR, Newman J, Snell EH.Acta Crystallogr F Struct Biol Commun. 2014 Aug;70(Pt 8):993-1008.
- Crystallization screening: the influence of history on current practice. Luft JR, Newman J, Snell EH. Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):835-53.
- Statistical analysis of crystallization database links protein physico-chemical features with crystallization mechanisms. Fusco D, Barnum TJ, Bruno AE, Luft JR, Snell EH, Mukherjee S, Charbonneau P. PLoS One. 2014 Jul 2;9(7):e101123.
- A new view on crystal harvesting. Luft JR, Grant TD, Wolfley JR, Snell EH. J Appl Crystallogr. 2014 May 29;47(Pt 3):1158-1161.
- Optical measurements of long-range protein vibrations. Acbas G, Niessen KA, Snell EH, Markelz AG. Nat Commun. 2014;5:3076.
- Neutron structure of the cyclic glucose-bound xylose isomerase E186Q mutant. Munshi P, Snell EH, van der Woerd MJ, Judge RA, Myles DA, Ren Z, Meilleur F. Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):414-20.
- The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA. Grant TD, Luft JR, Wolfley JR, Snell ME, Tsuruta H, Corretore S, Quartley E, Phizicky EM, Grayhack EJ, Snell EH. J Mol Biol. 2013 Jul 24;425(14):2480-93.
- Purification and SAXS analysis of the integrin linked kinase, PINCH, parvin (IPP) heterotrimeric complex. Stiegler AL, Grant TD, Luft JR, Calderwood DA, Snell EH, Boggon TJ. PLoS One. 2013;8(1):e55591.
- Insights into the mechanism of X-ray-induced disulfide-bond cleavage in lysozyme crystals based on EPR, optical absorption and X-ray diffraction studies. Sutton KA, Black PJ, Mercer KR, Garman EF, Owen RL, Snell EH, Bernhard WA. Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2381-94.
- On the need for an international effort to capture, share and use crystallization screening data. Newman J, Bolton EE, Müller-Dieckmann J, Fazio VJ, Gallagher DT, Lovell D, Luft JR, Peat TS, Ratcliffe D, Sayle RA, Snell EH, Taylor K, Vallotton P, Velanker S, von Delft F. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):253-8.
- Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase. Grant TD, Snell EH, Luft JR, Quartley E, Corretore S, Wolfley JR, Snell ME, Hadd A, Perona JJ, Phizicky EM, Grayhack EJ. Nucleic Acids Res. 2012 Apr;40(8):3723-31.
- What’s in a drop? Correlating observations and outcomes to guide macromolecular crystallization experiments. Luft JR, Wolfley JR, Snell EH. Cryst Growth Des. 2011 Mar 2;11(3):651-663.
- Lessons from high-throughput protein crystallization screening: 10 years of practical experience. Luft JR, Snell EH, Detitta GT. Expert Opin Drug Discov. 2011 May;6(5):465-80.
- Small angle X-ray scattering as a complementary tool for high-throughput structural studies. Grant TD, Luft JR, Wolfley JR, Tsuruta H, Martel A, Montelione GT, Snell EH. Biopolymers. 2011 Aug;95(8):517-30.
- Crystal cookery – using high-throughput technologies and the grocery store as a teaching tool. Luft JR, Furlani NM, Nemoyer RE, Penna EJ, Wolfley JR, Snell ME, Potter SA, Snell EH. J Appl Crystallogr. 2010 Oct 1;43(Pt 5):1189-1207.
- Macromolecular Crystallization and Crystal Perfection. Chayen, NE, Helliwell, JR, and Snell EH. IUCr Monographs in Crystallography Number 24, Oxford University Press (2010).
- Sliding clamp-DNA interactions are required for viability and contribute to DNA polymerase management in Escherichia coli. Heltzel JM, Scouten Ponticelli SK, Sanders LH, Duzen JM, Cody V, Pace J, Snell EH, Sutton MD. J Mol Biol. 2009 Mar 20;387(1):74-91.
- Establishing a training set through the visual analysis of crystallization trials. Part II: crystal examples. Snell EH, Lauricella AM, Potter SA, Luft JR, Gulde SM, Collins RJ, Franks G, Malkowski MG, Cumbaa C, Jurisica I, DeTitta GT. Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1131-7.
- Establishing a training set through the visual analysis of crystallization trials. Part I: approximately 150,000 images. Snell EH, Luft JR, Potter SA, Lauricella AM, Gulde SM, Malkowski MG, Koszelak-Rosenblum M, Said MI, Smith JL, Veatch CK, Collins RJ, Franks G, Thayer M, Cumbaa C, Jurisica I, Detitta GT. Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1123-30.
- Glycerol concentrations required for the successful vitrification of cocktail conditions in a high-throughput crystallization screen. Kempkes R, Stofko E, Lam K, Snell EH. Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):287-301.
- The application and use of chemical space mapping to interpret crystallization screening results. Snell EH, Nagel RM, Wojtaszcyk A, O’Neill H, Wolfley JL, Luft JR. Acta Crystallogr D Biol Crystallogr. 2008 Dec;64(Pt 12):1240-9.
- AutoSherlock: a program for effective crystallization data analysis. Nagel RM, Luft JR, Snell EH. J Appl Crystallogr. 2008 Dec 1;41(Pt 6):1173-1176.
- Glycerol concentrations required for the successful vitrification of cocktail conditions in a high-throughput crystallization screen. Kempkes R, Stofko E, Lam K, Snell EH. Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):287-301.
- Digital X-ray camera for quality evaluation three-dimensional topographic reconstruction of single crystals of biological macromolecules. Borgstahl, G., Lovelace, J., Snell, E.H., Bellamy, H. 7,466,798, Issue Dec. 16th 2008.
- Efficient optimization of crystallization conditions by manipulation of drop volume ratio and temperature. Luft JR, Wolfley JR, Said MI, Nagel RM, Lauricella AM, Smith JL, Thayer MH, Veatch CK, Snell EH, Malkowski MG, Detitta GT. Protein Sci. 2007 Apr;16(4):715-22.
- Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing. Juers DH, Lovelace J, Bellamy HD, Snell EH, Matthews BW, Borgstahl GE. Acta Crystallogr D Biol Crystallogr. 2007 Nov;63(Pt 11):1139-53.
- Non-invasive measurement of X-ray beam heating on a surrogate crystal sample. Snell EH, Bellamy HD, Rosenbaum G, van der Woerd MJ. J Synchrotron Radiat. 2007 Jan;14(Pt 1):109-15.
- Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation. Deng X, Habel JE, Kabaleeswaran V, Snell EH, Wold MS, Borgstahl GE. J Mol Biol. 2007 Dec 7;374(4):865-76.
- Optimizing crystal volume for neutron diffraction: D-xylose isomerase. Snell EH, van der Woerd MJ, Damon M, Judge RA, Myles DA, Meilleur F. Eur Biophys J. 2006 Sep;35(7):621-32.
- A quasi-Laue neutron crystallographic study of D-xylose isomerase. Meilleur F, Snell EH, van der Woerd MJ, Judge RA, Myles DA. Eur Biophys J. 2006 Sep;35(7):601-9.
- Finding a cold needle in a warm haystack: Infrared imaging applied to locating cryocooled crystals. Snell, EH, van der Woerd, MJ, Miller, MD and Deacon, AM. Journal of Applied Crystallography, 38, 69-77 (2005).
- Crystallization in Microgravity. Snell, EH, and Helliwell, JR. Macromolecular Reports on Progress in Physics, 68, 799-853 (2005).
- Extracting trends from two decades of microgravity macromolecular crystallization history. Judge RA, Snell EH, van der Woerd MJ. Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):763-71.
- Imaging modulated reflections from a semi-crystalline state of profiling:actin. Lovelace, JJ, Narayan, K, Chik, JK, Bellamy, HD, Snell, EH, Lindberg, U, Schutt, CE and Borgstahl, GEO.J. Applied Crystallography 37, 327-330 (2004).
- First results of digital topography applied to macromolecular crystals. Lovelace, JJ, Soares, A, Bellamy, HD, Sweet, RM, Snell, EH and Borgstahl, GEO. J. Applied Crystallography 37, 481-485 (2004).
- Physical and structural studies on the cryocooling of insulin crystals. Vahedi-Faridi A, Lovelace J, Bellamy HD, Snell EH, Borgstahl GE. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2169-82.
- Macromolecular crystal quality. Snell EH, Bellamy HD, Borgstahl GE. Methods Enzymol. 2003;368:268-88.
- The development and application of a method to quantify the quality of cryoprotectant conditions using standard area detector X-ray images. McFerrin, M and Snell, EH. J. Appl. Cryst. 35, 538-545 (2002).
- Seeing the heat — preliminary studies of cryocrystallography using infrared imaging. Snell EH, Judge RA, Larson M, van der Woerd MJ. J Synchrotron Radiat. 2002 Nov 1;9(Pt 6):361-7.
- Thaumatin crystallization aboard the International Space Station using liquid-liquid diffusion in the Enhanced Gaseous Nitrogen Dewar (EGN). Barnes CL, Snell EH, Kundrot CE.Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):751-60.
- Free-falling crystals: Biological macromolecular crystal growth studies in low earth orbit. Judge, RA., Snell, EH. and Pusey, ML. Dev. Chem. Eng. Mineral Process. 10(5/6) 479-488 (2002).
- Fluid Flows and Macromolecular Growth in Microgravity,Helliwell, JR, Snell, EH, Chayen, NE, Judge, RA, Boggon, TJ and Pusey, ML. Published in Physics of Fluids in Microgravity, ch 14, pages 489-514. Taylor and Francis. Editor, R. Monti (2002).
- Method for measurement of physical characteristics of crystals. Borgstahl, G., Lovelace, J., Snell, E.H. 6,498,829, Issue date Dec. 24th 2002.
- A test of macromolecular crystallization in microgravity: large well ordered insulin crystals. Borgstahl GE, Vahedi-Faridi A, Lovelace J, Bellamy HD, Snell EH. Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1204-7.
- Investigating the effect of impurities on macromolecule crystal growth in microgravity. Snell, EH, Judge, RA, Crawford, L, Forsythe, EL, Pusey, ML, Sportiello, M, Todd, P, Bellamy, H, Lovelace, J, Cassanto, Borgstahl, GEO. Crystal Growth and Design, 1, 2, 151-158 (2001).
- Microgravity and Macromolecular Crystallography. Kundrot, CE, Judge, RA, Pusey, ML, & Snell, EH. Crystal Growth and Design. Crystal Growth and Design, 1, 87-99 (2001).
- The high-mosaicity illusion: revealing the true physical characteristics of macromolecular crystals. Bellamy HD, Snell EH, Lovelace J, Pokross M, Borgstahl GE. Acta Crystallogr D Biol Crystallogr. (2000) Aug;56(Pt 8):986-95.
- BEAM-ish: A graphical user interface for the physical characterization of macromolecular crystals. Lovelace, J, Snell, EH, Pokross, M, Arvai, A, Nielsen, C, Nguyen, X, Bellamy, H and Borgstahl, GEO. J. Applied Crystallography, 33, 1187-1188 (2000).
- Synchrotron X-ray reciprocal-space mapping, topography and diffraction resolution studies of macromolecular crystal quality. Boggon TJ, Helliwell JR, Judge RA, Olczak A, Siddons DP, Snell EH, Stojanoff V.Acta Crystallogr D Biol Crystallogr. 2000 Jul;56(Pt 7):868-80.
- Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase. Borgstahl GE, Pokross M, Chehab R, Sekher A, Snell EH. J Mol Biol. 2000 Mar 3;296(4):951-9.
- Crystallization of chicken egg white lysozyme from assorted sulphate salts. EL Forsythe, EH Snell, CC Malone and ML Pusey. J.Cryst. Growth, 196, 332-343. (1999).
- The effect of temperature and solution pH on the nucleation of tetragonal lysozyme crystals. Judge RA, Jacobs RS, Frazier T, Snell EH, Pusey ML. Biophys J. 1999 Sep;77(3):1585-93.
- Crystallization of chicken egg-white lysozyme from ammonium sulfate. Forsythe EL, Snell EH, Pusey ML. Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):795-7.
- Crystallization of biological molecules in microgravity. Snell, EH, Chayen, NE and Helliwell, JR. The Biochemist, Vol 21, 6, 19-24 (1999).
- Protein crystal movements and fluid flows during microgravity growth. Boggon, TJ, Chayen, NE, Snell, EH, Dong, J, Lautenschlager, P, Potthast, L, Siddons, DP, Stojanoff, V, Gordon, E, Thompson, AW, Zagalsky, PF, Bi, R-C, and Helliwell, JR. Phil. Trans. R. Soc. Lond. A.356, 1045-1061 (1998).
- Quality evaluation of macromolecular crystals using X-ray mosaicity measurements. Snell, E.H. Proceedings of the Montreal Spacebound 1997 meeting, Canadian Space Agency, 306-315. (1998).
- Ho JX, Snell EH, Sisk RC, Ruble JR, Carter DC, Owens SM, Gibson WM. Stationary crystal diffraction with a monochromatic convergent X-ray source and application for macromolecular crystal data collection. Acta Crystallogr D Biol Crystallogr. 1998 Mar 1;54(Pt 2):200-14.
- CCD video observation of microgravity crystallization of lysozyme and correlation with accelerometer data. Snell EH, Boggon TJ, Helliwell JR, Moskowitz ME, Nadarajah A. Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):747-55.
- Partial improvement of crystal quality for microgravity-grown apocrustacyanin C1. Snell EH, Cassetta A, Helliwell JR, Boggon TJ, Chayen NE, Weckert E, Holzer K, Schroer K, Gordon EJ, Zagalsky PF. Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):231-9.
- CCD video observation of microgravity crystallization: apocrustacyanin C1. Chayen, NE, Snell, EH, Helliwell, JR and Zagalsky, PF. J. Cryst. Growth 171, 219-225 (1997).
- Lysozyme crystal growth kinetics monitored using a Mach-Zehnder interferometer. Snell EH, Helliwell JR, Boggon TJ, Lautenschlager P, Potthast L. Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):529-33.
- An Investigation of the perfection of lysozyme protein crystals grown in microgravity and on earth. Helliwell, JR, Snell, EH, & Weisgerber, S. Springer Lecture notes in Physics. Vol 464, Ch. 30 edited by Ratke, L., Walter, H. & Feuerbache, B. Springer Verlag, 155-170 (1996).
- X-ray topography: An old technique with a new application. Stojanoff, V, Siddons, DP, Snell, EH and Helliwell, JR. Synchrotron Radiation News 9, 25-26 (1996).
- Trends and challenges in experimental macromolecular crystallography. Chayen NE, Boggon TJ, Cassetta A, Deacon A, Gleichmann T, Habash J, Harrop SJ, Helliwell JR, Nieh YP, Peterson MR, Raftery J, Snell EH, Hädener A, Niemann AC, Siddons DP, Stojanoff V, Thompson AW, Ursby T, Wulff M. Q Rev Biophys. 1996.
- Improvements in lysozyme protein crystal perfection through microgravity growth. Snell EH, Weisgerber S, Helliwell JR, Hölzer K, Schroer K. Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1099-102.
- Time resolved biological and pertubation chemical crystallography: Laue and monochromatic developments. Bradbrook, G, Deacon, A, Habash, J, Helliwell, JR, Helliwell, M, Nieh, YP, Snell, EH, Trapini, S, Thompson, AW, Campbell, JW, Allinson, NM, Moon, K, Ursby, T, and Wulff, M. SPIE 2521, 160-177 (1995).
- Image-Plate Synchrotron Laue Data Collection and Subsequent Structural Analysis of a Small Test Crystal of a Nickel-Containing Aluminophosphate. Snell E, Habash J, Helliwell M, Helliwell JR, Raftery J, Kaucic V and Campbell JW. Journal of Synchrotron Radiation, 2, 22-26 (1995).
- Electron density maps of lysozyme calculated using synchrotron Laue data comprising singles and deconvoluted multiples. Campbell , JW, deacon, A, Habash, J, Helliwell, JR, McSweeney, S, Quan, H, Raftery, J and Snell, E. Bull. Mater. Sci., 17,1, 1-18 (1994).
- The emergence of the synchrotron Laue method for rapid data collection from protein crystals. Cassetta, A, Deacon, A, Emmerich, C, Habash, J, Helliwell, JR, McSweeney, S, Snell, E, Thompson, AW and Weisgerber, S. Proc. R. Soc. Lond. A, 177-192 (1993).
- John Moores University of Liverpool, UK, Physics, B.Sc. Hons (1st).
- University of Manchester, UK, Chemistry, Ph.D.
- NASA Biophysics Laboratory, Marshall Space Flight Center, USA, National Research Council Fellow.