Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction
1990; Royal Society; Volume: 241; Issue: 1300 Linguagem: Inglês
10.1098/rspb.1990.0057
ISSN1471-2954
Autores Tópico(s)Advanced X-ray Imaging Techniques
ResumoRestricted accessMoreSectionsView PDF ToolsAdd to favoritesDownload CitationsTrack Citations ShareShare onFacebookTwitterLinked InRedditEmail Cite this article Henderson Richard 1990Cryo-protection of protein crystals against radiation damage in electron and X-ray diffractionProc. R. Soc. Lond. B.2416–8http://doi.org/10.1098/rspb.1990.0057SectionRestricted accessArticleCryo-protection of protein crystals against radiation damage in electron and X-ray diffraction Richard Henderson Google Scholar Find this author on PubMed Search for more papers by this author Richard Henderson Google Scholar Find this author on PubMed Published:23 July 1990https://doi.org/10.1098/rspb.1990.0057AbstractBy using the fading of electron diffraction patterns during electron irradiation of protein or other organic crystals as a benchmark to measure destruction of the crystalline atomic arrangement by ionizing radiation, calculations suggest that protein crystals in laboratory X-ray beams might last for about five years when the specimen is cooled to liquid nitrogen temperatures or below. It is suggested that all crystals should be equally stable to X-irradiation at this temperature, as they are to electron irradiation. The calculation, which depends on the assumption that electrons and X-rays are more or less equally damaging to the structure giving rise to the diffraction at very low temperature, supports experimental observations that X-ray diffraction from protein crystals seems to last indefinitely at liquid nitrogen temperatures, even in the most powerful beams available at synchrotron X-ray sources. An attempt is made to explain the relation between the present analysis and other ways of viewing radiation damage.FootnotesThis text was harvested from a scanned image of the original document using optical character recognition (OCR) software. As such, it may contain errors. Please contact the Royal Society if you find an error you would like to see corrected. Mathematical notations produced through Infty OCR. 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Marín‐Tovar Y, Serrano‐Posada H, Díaz‐Vilchis A and Rudiño‐Piñera E (2022) PCNA from Thermococcus gammatolerans : A protein involved in chromosomal DNA metabolism intrinsically resistant at high levels of ionizing radiation , Proteins: Structure, Function, and Bioinformatics, 10.1002/prot.26346, 90:9, (1684-1698), Online publication date: 1-Sep-2022. Xue H, Zhang M, Liu J, Wang J and Ren G (2022) Cryo-electron tomography related radiation-damage parameters for individual-molecule 3D structure determination, Frontiers in Chemistry, 10.3389/fchem.2022.889203, 10 Yabukarski F, Doukov T, Mokhtari D, Du S and Herschlag D (2022) Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals, Acta Crystallographica Section D Structural Biology, 10.1107/S2059798322005939, 78:8, (945-963), Online publication date: 1-Aug-2022. Gopalasingam C and Hasnain S (2022) Frontiers in metalloprotein crystallography and cryogenic electron microscopy, Current Opinion in Structural Biology, 10.1016/j.sbi.2022.102420, 75, (102420), Online publication date: 1-Aug-2022. Rose S, Baba S, Okumura H, Antonyuk S, Sasaki D, Hedison T, Shanmugam M, Heyes D, Scrutton N, Kumasaka T, Tosha T, Eady R, Yamamoto M and Hasnain S (2022) Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases, Proceedings of the National Academy of Sciences, 10.1073/pnas.2205664119, 119:30, Online publication date: 26-Jul-2022. Liang B, Zhang Y, Leist C, Ou Z, Položij M, Wang Z, Mücke D, Dong R, Zheng Z, Heine T, Feng X, Kaiser U and Qi H (2022) Optimal acceleration voltage for near-atomic resolution imaging of layer-stacked 2D polymer thin films, Nature Communications, 10.1038/s41467-022-31688-4, 13:1 Latychevskaia T and Kohli A (2022) Low-dose shift- and rotation-invariant diffraction recognition imaging, Scientific Reports, 10.1038/s41598-022-15486-y, 12:1 Naydenova K, Kamegawa A, Peet M, Henderson R, Fujiyoshi Y and Russo C (2022) On the reduction in the effects of radiation damage to two-dimensional crystals of organic and biological molecules at liquid-helium temperature, Ultramicroscopy, 10.1016/j.ultramic.2022.113512, 237, (113512), Online publication date: 1-Jul-2022. Levitz T, Weckener M, Fong I, Naismith J, Drennan C, Brignole E, Clare D and Darrow M (2022) Approaches to Using the Chameleon: Robust, Automated, Fast-Plunge cryoEM Specimen Preparation, Frontiers in Molecular Biosciences, 10.3389/fmolb.2022.903148, 9 Ogawa Y and Putaux J (2022) Recent Advances in Electron Microscopy of Carbohydrate Nanoparticles, Frontiers in Chemistry, 10.3389/fchem.2022.835663, 10 Jang K, Kim H, Hlaing S, Kang M, Choe H and Kim Y (2022) A Short Review on Cryoprotectants for 3D Protein Structure Analysis, Crystals, 10.3390/cryst12020138, 12:2, (138) Ruiz-González M, Torres-Pardo A and González-Calbet J (2021) The Role of Transmission Electron Microscopy in the Early Development of Mesoporous Materials for Tissue Regeneration and Drug Delivery Applications, Pharmaceutics, 10.3390/pharmaceutics13122200, 13:12, (2200) Tuieng R, Cartmell S, Kirwan C and Sherratt M (2021) The Effects of Ionising and Non-Ionising Electromagnetic Radiation on Extracellular Matrix Proteins, Cells, 10.3390/cells10113041, 10:11, (3041) Egerton R (2021) Dose measurement in the TEM and STEM, Ultramicroscopy, 10.1016/j.ultramic.2021.113363, 229, (113363), Online publication date: 1-Oct-2021. Woodruff D (2021) Synchrotron Radiation Fernando N, Cairns A, Murray C, Thompson A, Dickerson J, Garman E, Ahmed N, Ratcliff L and Regoutz A (2021) Structural and Electronic Effects of X-ray Irradiation on Prototypical [M(COD)Cl] 2 Catalysts , The Journal of Physical Chemistry A, 10.1021/acs.jpca.1c05759, 125:34, (7473-7488), Online publication date: 2-Sep-2021. Zhang Y, Lu P, Rotunno E, Troiani F, van Schayck J, Tavabi A, Dunin-Borkowski R, Grillo V, Peters P and Ravelli R (2021) Single-particle cryo-EM: alternative schemes to improve dose efficiency, Journal of Synchrotron Radiation, 10.1107/S1600577521007931, 28:5, (1343-1356), Online publication date: 1-Sep-2021. Kristensen L, Holton J, Rad B, Chen Y, Petzold C, Gupta S and Ralston C (2021) Hydroxyl radical mediated damage of proteins in low oxygen solution investigated using X-ray footprinting mass spectrometry, Journal of Synchrotron Radiation, 10.1107/S1600577521004744, 28:5, (1333-1342), Online publication date: 1-Sep-2021. Wityk P, Kostrzewa-Nowak D, Krawczyk B, Michalik M and Nowak R (2021) X-ray and UV Radiation Damage of dsDNA/Protein Complexes, Molecules, 10.3390/molecules26113132, 26:11, (3132) Du M, Di Z, Gürsoy D, Xian R, Kozorovitskiy Y and Jacobsen C (2021) Upscaling X-ray nanoimaging to macroscopic specimens, Journal of Applied Crystallography, 10.1107/S1600576721000194, 54:2, (386-401), Online publication date: 1-Apr-2021. Kato K, Miyazaki N, Hamaguchi T, Nakajima Y, Akita F, Yonekura K and Shen J (2021) High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams, Communications Biology, 10.1038/s42003-021-01919-3, 4:1 Zhao R, Liu H, Li Y, Guo M and Zhang X (2021) Catalytic Nanozyme for Radiation Protection, Bioconjugate Chemistry, 10.1021/acs.bioconjchem.0c00648, 32:3, (411-429), Online publication date: 17-Mar-2021. Beckers M, Mann D and Sachse C (2021) Structural interpretation of cryo-EM image reconstructions, Progress in Biophysics and Molecular Biology, 10.1016/j.pbiomolbio.2020.07.004, 160, (26-36), Online publication date: 1-Mar-2021. Takaba K, Maki-Yonekura S, Inoue S, Hasegawa T and Yonekura K (2021) Protein and Organic-Molecular Crystallography With 300kV Electrons on a Direct Electron Detector, Frontiers in Molecular Biosciences, 10.3389/fmolb.2020.612226, 7 Fischer M (2021) Macromolecular room temperature crystallography, Quarterly Reviews of Biophysics, 10.1017/S0033583520000128, 54, . Latychevskaia T (2021) Phase retrieval methods applied to coherent imaging , 10.1016/bs.aiep.2021.04.001, (1-62), . Aller P and Orville A (2021) Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources Structural Proteomics, 10.1007/978-1-0716-1406-8_11, (203-228), . Hattne J (2021) Low-Dose Data Collection and Radiation Damage in MicroED cryoEM, 10.1007/978-1-0716-0966-8_15, (309-319), . Dickerson J and Garman E (2020) Doses for experiments with microbeams and microcrystals: Monte Carlo simulations in RADDOSE‐3D , Protein Science, 10.1002/pro.3922, 30:1, (8-19), Online publication date: 1-Jan-2021. Mehr A, Henneberg F, Chari A, Görlich D and Huyton T (2020) The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography, Acta Crystallographica Section D Structural Biology, 10.1107/S2059798320013741, 76:12, (1222-1232), Online publication date: 1-Dec-2020. Doukov T, Herschlag D and Yabukarski F (2020) Instrumentation and experimental procedures for robust collection of X-ray diffraction data from protein crystals across physiological temperatures, Journal of Applied Crystallography, 10.1107/S1600576720013503, 53:6, (1493-1501), Online publication date: 1-Dec-2020. Kim J, Lee C, Lim S, Andring J, Adhikari A, McKenna R and Kim C (2020) Structural insights into the effect of active-site mutation on the catalytic mechanism of carbonic anhydrase, IUCrJ, 10.1107/S2052252520011008, 7:6, (985-994), Online publication date: 1-Nov-2020. Gong X, Gnanasekaran K, Chen Z, Robison L, Wasson M, Bentz K, Cohen S, Farha O and Gianneschi N (2020) Insights into the Structure and Dynamics of Metal–Organic Frameworks via Transmission Electron Microscopy, Journal of the American Chemical Society, 10.1021/jacs.0c08773, 142:41, (17224-17235), Online publication date: 14-Oct-2020. Naydenova K, Jia P and Russo C (2020) Cryo-EM with sub–1 Å specimen movement, Science, 10.1126/science.abb7927, 370:6513, (223-226), Online publication date: 9-Oct-2020. Kim J, Lee C, Lim S, Adhikari A, Andring J, McKenna R, Ghim C and Kim C (2020) Elucidating the role of metal ions in carbonic anhydrase catalysis, Nature Communications, 10.1038/s41467-020-18425-5, 11:1 Bhattacharyya R, Dhar J, Ghosh Dastidar S, Chakrabarti P and Weiss M (2020) The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions, IUCrJ, 10.1107/S2052252520008520, 7:5, (825-834), Online publication date: 1-Sep-2020. Pfanzagl V, Beale J, Michlits H, Schmidt D, Gabler T, Obinger C, Djinović-Carugo K and Hofbauer S (2020) X-ray–induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner, Journal of Biological Chemistry, 10.1074/jbc.RA120.014087, 295:39, (13488-13501), Online publication date: 1-Sep-2020. Müh F and Zouni A (2020) Structural basis of light‐harvesting in the photosystem II core complex, Protein Science, 10.1002/pro.3841, 29:5, (1090-1119), Online publication date: 1-May-2020. Montanha G, Rodrigues E, Marques J, de Almeida E, dos Reis A and Pereira de Carvalho H (2019) X-ray fluorescence spectroscopy (XRF) applied to plant science: challenges towards in vivo analysis of plants , Metallomics, 10.1039/c9mt00237e, 12:2, (183-192), Online publication date: 26-Feb-2020. de la Mora E, Coquelle N, Bury C, Rosenthal M, Holton J, Carmichael I, Garman E, Burghammer M, Colletier J and Weik M (2020) Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures, Proceedings of the National Academy of Sciences, 10.1073/pnas.1821522117, 117:8, (4142-4151), Online publication date: 25-Feb-2020. Liu L (2020) Methods: Experimental Techniques and Data Science Chemistry in Action: Making Molecular Movies with Ultrafast Electron Diffraction and Data Science, 10.1007/978-3-030-54851-3_2, (9-63), . Wakatsuki S (2020) Structural Biology Applications of Synchrotron Radiation and X-Ray Free-Electron Lasers Synchrotron Light Sources and Free-Electron Lasers, 10.1007/978-3-030-23201-6_44, (1673-1716), . Zachman M, de Jonge N, Fischer R, Jungjohann K and Perea D (2019) Cryogenic specimens for nanoscale characterization of solid–liquid interfaces, MRS Bulletin, 10.1557/mrs.2019.289, 44:12, (949-955), Online publication date: 1-Dec-2019. Tai Y, Takaba K, Hanazono Y, Dao H, Miki K and Takeda K (2019) X-ray crystallographic studies on the hydrogen isotope effects of green fluorescent protein at sub-ångström resolutions, Acta Crystallographica Section D Structural Biology, 10.1107/S2059798319014608, 75:12, (1096-1106), Online publication date: 1-Dec-2019. Pfeil-Gardiner O, Mills D, Vonck J and Kuehlbrandt W (2019) A comparative study of single-particle cryo-EM with liquid-nitrogen and liquid-helium cooling, IUCrJ, 10.1107/S2052252519011503, 6:6, (1099-1105), Online publication date: 1-Nov-2019. Atakisi H, Conger L, Moreau D and Thorne R (2019) Resolution and dose dependence of radiation damage in biomolecular systems, IUCrJ, 10.1107/S2052252519008777, 6:6, (1040-1053), Online publication date: 1-Nov-2019. Tolstikova A, Levantino M, Yefanov O, Hennicke V, Fischer P, Meyer J, Mozzanica A, Redford S, Crosas E, Opara N, Barthelmess M, Lieske J, Oberthuer D, Wator E, Mohacsi I, Wulff M, Schmitt B, Chapman H and Meents A (2019) 1 kHz fixed-target serial crystallography using a multilayer monochromator and an integrating pixel detector, IUCrJ, 10.1107/S205225251900914X, 6:5, (927-937), Online publication date: 1-Sep-2019. Stellato F, Chiaraluce R, Consalvi V, De Santis E, La Penna G, Proux O, Rossi G and Morante S (2019) Dealing with Cu reduction in X-ray absorption spectroscopy experiments, Metallomics, 10.1039/c9mt00110g, 11:8, (1401-1410), Online publication date: 1-Aug-2019. Hood Z and Chi M (2019) Mechanistic understanding and strategies to design interfaces of solid electrolytes: insights gained from transmission electron microscopy, Journal of Materials Science, 10.1007/s10853-019-03633-2, 54:15, (10571-10594), Online publication date: 1-Aug-2019. Guo G, Zhu P, Fuchs M, Shi W, Andi B, Gao Y, Hendrickson W, McSweeney S and Liu Q (2019) Synchrotron microcrystal native-SAD phasing at a low energy, IUCrJ, 10.1107/S2052252519004536, 6:4, (532-542), Online publication date: 1-Jul-2019. Nicolas J, Aeffner S and Salditt T (2019) Radiation damage studies in cardiac muscle cells and tissue using microfocused X-ray beams: experiment and simulation, Journal of Synchrotron Radiation, 10.1107/S1600577519006817, 26:4, (980-990), Online publication date: 1-Jul-2019. Baslé A and Lewis R (2019) Principles and Practice in Macromolecular X-Ray Crystallography Biomolecular and Bioanalytical Techniques, 10.1002/9781119483977.ch16, (385-419) Takaba K, Tai Y, Eki H, Dao H, Hanazono Y, Hasegawa K, Miki K and Takeda K (2019) Subatomic resolution X-ray structures of green fluorescent protein, IUCrJ, 10.1107/S205225251900246X, 6:3, (387-400), Online publication date: 1-May-2019. Yonekura K, Ishikawa T and Maki-Yonekura S (2019) A new cryo-EM system for electron 3D crystallography by eEFD, Journal of Structural Biology, 10.1016/j.jsb.2019.03.009, 206:2, (243-253), Online publication date: 1-May-2019. Zárate-Romero A, Stojanoff V, Cohen A, Hansberg W and Rudiño-Piñera E (2019) X-ray driven reduction of Cpd I of Catalase-3 from N. crassa reveals differential sensitivity of active sites and formation of ferrous state, Archives of Biochemistry and Biophysics, 10.1016/j.abb.2019.03.020, 666, (107-115), Online publication date: 1-May-2019. Cianci M, Nanao M and Schneider T (2019) Long-wavelength Mesh&Collect native SAD phasing from microcrystals , Acta Crystallographica Section D Structural Biology, 10.1107/S2059798319002031, 75:2, (192-199), Online publication date: 1-Feb-2019. Campbell G, McKeown J and Santala M (2019) High-Speed Electron Microscopy Springer Handbook of Microscopy, 10.1007/978-3-030-00069-1_8, (455-486), . Rodrigues E, Gomes M, Duran N, Cassanji J, da Cruz T, Sant'Anna Neto A, Savassa S, de Almeida E and Carvalho H (2018) Laboratory Microprobe X-Ray Fluorescence in Plant Science: Emerging Applications and Case Studies, Frontiers in Plant Science, 10.3389/fpls.2018.01588, 9 Gao Y, Xu W, Shi W, Soares A, Jakoncic J, Myers S, Martins B, Skinner J, Liu Q, Bernstein H, McSweeney S, Nazaretski E and Fuchs M (2018) High-speed raster-scanning synchrotron serial microcrystallography with a high-precision piezo-scanner, Journal of Synchrotron Radiation, 10.1107/S1600577518010354, 25:5, (1362-1370), Online publication date: 1-Sep-2018. Henderson R (2018) From Electron Crystallography to Single Particle CryoEM (Nobel Lecture), Angewandte Chemie International Edition, 10.1002/anie.201802731, 57:34, (10804-10825), Online publication date: 20-Aug-2018. Henderson R (2018) Von der Elektronenkristallographie zur Einzelpartikel-KryoEM (Nobel-Aufsatz), Angewandte Chemie, 10.1002/ange.201802731, 130:34, (10966-10989), Online publication date: 20-Aug-2018. Bekx J, Son S, Santra R and Ziaja B (2018) Ab initio calculation of electron-impact-ionization cross sections for ions in exotic electron configurations , Physical Review A, 10.1103/PhysRevA.98.022701, 98:2 Wherland S and Pecht I (2018) Radiation chemists look at damage in redox proteins induced by X-rays, Proteins: Structure, Function, and Bioinformatics, 10.1002/prot.25521, 86:8, (817-826), Online publication date: 1-Aug-2018. Borek D, Bromberg R, Hattne J and Otwinowski Z (2018) Real-space analysis of radiation-induced specific changes with independent component analysis, Journal of Synchrotron Radiation, 10.1107/S1600577517018148, 25:2, (451-467), Online publication date: 1-Mar-2018. Kubin M, Kern J, Guo M, Källman E, Mitzner R, Yachandra V, Lundberg M, Yano J and Wernet P (2018) X-ray-induced sample damage at the Mn L-edge: a case study for soft X-ray spectroscopy of transition metal complexes in solution, Physical Chemistry Chemical Physics, 10.1039/C8CP03094D, 20:24, (16817-16827) Du M and Jacobsen C (2018) Relative merits and limiting factors for x-ray and electron microscopy of thick, hydrated organic materials, Ultramicroscopy, 10.1016/j.ultramic.2017.10.003, 184, (293-309), Online publication date: 1-Jan-2018. Bury C, Brooks-Bartlett J, Walsh S and Garman E (2017) Estimate your dose: RADDOSE-3D, Protein Science, 10.1002/pro.3302, 27:1, (217-228), Online publication date: 1-Jan-2018. Abela R, Beaud P, van Bokhoven J, Chergui M, Feurer T, Haase J, Ingold G, Johnson S, Knopp G, Lemke H, Milne C, Pedrini B, Radi P, Schertler G, Standfuss J, Staub U and Patthey L (2017) Perspective: Opportunities for ultrafast science at SwissFEL, Structural Dynamics, 10.1063/1.4997222, 4:6, (061602), Online publication date: 1-Nov-2017. Aurelius O, Duman R, El Omari K, Mykhaylyk V and Wagner A (2017) Long-wavelength macromolecular crystallography – First successful native SAD experiment close to the sulfur edge, Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms, 10.1016/j.nimb.2016.12.005, 411, (12-16), Online publication date: 1-Nov-2017. Dilanian R, Streltsov V, Coughlan H, Quiney H, Martin A, Klonis N, Dogovski C, Boutet S, Messerschmidt M, Williams G, Williams S, Phillips N, Nugent K, Tilley L and Abbey B (2017) Nanocrystallography measurements of early stage synthetic malaria pigment, Journal of Applied Crystallography, 10.1107/S1600576717012663, 50:5, (1533-1540), Online publication date: 1-Oct-2017. Vonck J and Mills D (2017) Advances in high-resolution cryo-EM of oligomeric enzymes, Current Opinion in Structural Biology, 10.1016/j.sbi.2017.05.016, 46, (48-54), Online publication date: 1-Oct-2017. Chergui M and Thomas J (2017) From structure to structural dynamics: Ahmed Zewail's legacy, Structural Dynamics, 10.1063/1.4998243, 4:4, (043802), Online publication date: 1-Jul-2017. Ohno H, Takeda K, Niwa S, Tsujinaka T, Hanazono Y, Hirano Y, Miki K and Pereira I (2017) Crystallographic characterization of the high-potential iron-sulfur protein in the oxidized state at 0.8 Å resolution, PLOS ONE, 10.1371/journal.pone.0178183, 12:5, (e0178183) Hegde R, Fedorov A, Sauder J, Burley S, Almo S and Ramagopal U (2017) The hidden treasure in your data: phasing with unexpected weak anomalous scatterers from routine data sets, Acta Crystallographica Section F Structural Biology Communications, 10.1107/S2053230X17002680, 73:4, (184-195), Online publication date: 1-Apr-2017. Deng J, Vine D, Chen S, Jin Q, Nashed Y, Peterka T, Vogt S and Jacobsen C (2017) X-ray ptychographic and fluorescence microscopy of frozen-hydrated cells using continuous scanning, Scientific Reports, 10.1038/s41598-017-00569-y, 7:1 Gati C, Oberthuer D, Yefanov O, Bunker R, Stellato F, Chiu E, Yeh S, Aquila A, Basu S, Bean R, Beyerlein K, Botha S, Boutet S, DePonte D, Doak R, Fromme R, Galli L, Grotjohann I, James D, Kupitz C, Lomb L, Messerschmidt M, Nass K, Rendek K, Shoeman R, Wang D, Weierstall U, White T, Williams G, Zatsepin N, Fromme P, Spence J, Goldie K, Jehle J, Metcalf P, Barty A and Chapman H (2017) Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser, Proceedings of the National Academy of Sciences, 10.1073/pnas.1609243114, 114:9, (2247-2252), Online publication date: 28-Feb-2017. Takaba K, Takeda K, Kosugi M, Tamada T and Miki K (2017) Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase, Scientific Reports, 10.1038/srep43162, 7:1 Bury C, Carmichael I and Garman E (2017) OH cleavage from tyrosine: debunking a myth, Journal of Synchrotron Radiation, 10.1107/S1600577516016775, 24:1, (7-18), Online publication date: 1-Jan-2017. Hasegawa K, Yamashita K, Murai T, Nuemket N, Hirata K, Ueno G, Ago H, Nakatsu T, Kumasaka T and Yamamoto M (2017) Development of a dose-limiting data collection strategy for serial synchrotron rotation crystallography, Journal of Synchrotron Radiation, 10.1107/S1600577516016362, 24:1, (29-41), Online publication date: 1-Jan-2017. Garman E and Weik M (2017) Radiation Damage in Macromolecular Crystallography Protein Crystallography, 10.1007/978-1-4939-7000-1_20, (467-489), . Diederichs K and Wang M (2017) Serial Synchrotron X-Ray Crystallography (SSX) Protein Crystallography, 10.1007/978-1-4939-7000-1_10, (239-272), . Noh D, Kim C, Kim Y and Song C (2016) Enhancing resolution in coherent x-ray diffraction imaging, Journal of Physics: Condensed Matter, 10.1088/0953-8984/28/49/493001, 28:49, (493001), Online publication date: 14-Dec-2016. Casanas A, Warshamanage R, Finke A, Panepucci E, Olieric V, Nöll A, Tampé R, Brandstetter S, Förster A, Mueller M, Schulze-Briese C, Bunk O and Wang M (2016) EIGER detector: application in macromolecular crystallography, Acta Crystallographica Section D Structural Biology, 10.1107/S2059798316012304, 72:9, (1036-1048), Online publication date: 1-Sep-2016. Wang J (2016) X-ray radiation-induced addition of oxygen atoms to protein residues, Protein Science, 10.1002/pro.2934, 25:8, (1407-1419), Online publication date: 1-Aug-2016. Horrell S, Antonyuk S, Eady R, Hasnain S, Hough M and Strange R (2016) Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal, IUCrJ, 10.1107/S205225251600823X, 3:4, (271-281), Online publication date: 1-Jul-2016. Rose J and Wang B (2016) SAD phasing: History, current impact and future opportunities, Archives of Biochemistry and Biophysics, 10.1016/j.abb.2016.03.018, 602, (80-94), Online publication date: 1-Jul-2016. Liebschner D, Yamada Y, Matsugaki N, Senda M and Senda T (2016) On the influence of crystal size and wavelength on native SAD phasing, Acta Crystallographica Section D Structural Biology, 10.1107/S2059798316005349, 72:6, (728-741), Online publication date: 1-Jun-2016. Roedig P, Duman R, Sanchez-Weatherby J, Vartiainen I, Burkhardt A, Warmer M, David C, Wagner A and Meents A (2016) Room-temperature macromolecular crystallography using a micro-patterned silicon chip with minimal background scattering, Journal of Applied Crystallography, 10.1107/S1600576716006348, 49:3, (968-975), Online publication date: 1-Jun-2016. Sato-Tomita A, Shibayama N, Happo N, Kimura K, Okabe T, Matsushita T, Park S, Sasaki Y and Hayashi K (2016) Development of an X-ray fluorescence holographic measurement system for protein crystals, Review of Scientific Instruments, 10.1063/1.4953453, 87:6, (063707), Online publication date: 1-Jun-2016. Kim C, Song H, Avvaru B, Gruner S, Park S and McKenna R (2016) Tracking solvent and protein movement during CO 2 release in carbonic anhydrase II crystals , Proceedings of the National Academy of Sciences, 10.1073/pnas.1520786113, 113:19, (5257-5262), Online publication date: 10-May-2016. Bowman S, Bridwell-Rabb J and Drennan C (2016) Metalloprotein Crystallography: More than a Structure, Accounts of Chemical Research, 10.1021/acs.accounts.5b00538, 49:4, (695-702), Online publication date: 19-Apr-2016. Tizei L, Lin Y, Lu A, Li L and Suenaga K (2016) Electron energy loss spectroscopy of excitons in two-dimensional-semiconductors as a function of temperature, Applied Physics Letters, 10.1063/1.4947058, 108:16, (163107), Online publication date: 18-Apr-2016. Cianci M, Groves M, Barford D and Schneider T (2016) Data collection with a tailored X-ray beam size at 2.69 Å wavelength (4.6 keV): sulfur SAD phasing of Cdc23 Nterm , Acta Crystallographica Section D Structural Biology, 10.1107/S2059798315010268, 72:3, (403-412), Online publication date: 1-Mar-2016. Bernasconi L and Brandao-Neto J (2016) Radiation damage in X-ray crystallography: a quantum-mechanical study of photoinduced defect formation in beeswax-analogue n-eicosane crystals, Theoretical Chemistry Accounts, 10.1007/s00214-015-1779-3, 135:2, Online publication date: 1-Feb-2016. Huang C, Olieric V, Ma P, Howe N, Vogeley L, Liu X, Warshamanage R, Weinert T, Panepucci E, Kobilka B, Diederichs K, Wang M and Caffrey M (2016) In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures , Acta Crystallographica Section D Structural Biology, 10.1107/S2059798315021683, 72:1, (93-112), Online publication date: 1-Jan-2016. Vinothkumar K and Henderson R (2016) Single particle electron cryomicroscopy: trends, issues and future perspective, Quarterly Reviews of Biophysics, 10.1017/S0033583516000068, 49, . Leontowich A, Hitchcock A and Egerton R (2016) Radiation damage yields across the carbon 1s excitation edge, Journal of Electron Spectroscopy and Related Phenomena, 10.1016/j.elspec.2015.11.010, 206, (58-64), Online publication date: 1-Jan-2016. Glaeser R (2016) Specimen Behavior in the Electron Beam The Resolution Revolution: Recent Advances In cryoEM, 10.1016/bs.mie.2016.04.010, (19-50), . Wakatsuki S (2016) Structural Biology Applications of Synchrotron Radiation and X-Ray Free-Electron Lasers Synchrotron Light Sources and Free-Electron Lasers, 10.1007/978-3-319-14394-1_44, (1421-1464), . Finke A, Panepucci E, Vonrhein C, Wang M, Bricogne G and Oliéric V (2016) Advanced Crystallographic Data Collection Protocols for Experimental Phasing Nucleic Acid Crystallography, 10.1007/978-1-4939-2763-0_11, (175-191), . Zander U, Bourenkov G, Popov A, de Sanctis D, Svensson O, McCarthy A, Round E, Gordeliy V, Mueller-Dieckmann C and Leonard G (2015) MeshAndCollect : an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines , Acta Crystallographica Section D Biological Crystallography, 10.1107/S1399004715017927, 71:11, (2328-2343), Online publication date: 1-Nov-2015. Sousa C, Carpentier
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