Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser

doi:10.1073/pnas.1609243114

	Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser
	Gati, Cornelius 1,14; Oberthuer, Dominik 1; Yefanov, Oleksandr 1; Bunker, Richard D.2,15; Stellato, Francesco 1; Chiu, Elaine 2; Yeh, Shin-Mei 2; Aquila, Andrew 1,3; Basu, Shibom 4,5,16; Bean, Richard 1,3; Beyerlein, Kenneth R.1; Botha, Sabine 6,17; Boutet, Sebastien 7; DePonte, Daniel P.1,8; Doak, R. Bruce 6,9; Fromme, Raimund 4,5; Galli, Lorenzo 1; Grotjohann, Ingo 4; James, Daniel R.9; Kupitz, Christopher 4,5,18; Lomb, Lukas 6; Messerschmidt, Marc 7,19; Nass, Karol 1,20; Rendek, Kimberly 4; Shoeman, Robert L.6; Wang, Dingjie9,21 ; Weierstall, Uwe 5,9; White, Thomas A.1; Williams, Garth J.7; Zatsepin, Nadia A.5,9; Fromme, Petra 2,4,5; Spence, John C. H.5,9; Goldie, Kenneth N.10; Jehle, Johannes A.11; Metcalf, Peter 2; Barty, Anton 1; Chapman, Henry N.1,12,13
	2017-02-28
发表期刊	PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (IF:9.4[JCR-2023],10.8[5-Year])
ISSN	0027-8424
卷号	114 期号:9 页码:2247-2252
发表状态	已发表
DOI	10.1073/pnas.1609243114
摘要	To understand how molecules function in biological systems, new methods are required to obtain atomic resolution structures from biological material under physiological conditions. Intense femtosecond- duration pulses fromX-ray free-electron lasers (XFELs) can outrun most damage processes, vastly increasing the tolerable dose before the specimen is destroyed. This in turn allows structure determination from crystals much smaller and more radiation sensitive than previously considered possible, allowing data collection from room temperature structures and avoiding structural changes due to cooling. Regardless, high-resolution structures obtained from XFEL data mostly use crystals far larger than 1 mu m(3) in volume, whereas the X-ray beam is often attenuated to protect the detector from damage caused by intense Bragg spots. Here, we describe the 2 resolution structure of native nanocrystalline granulovirus occlusion bodies (OBs) that are less than 0.016 mu m(3) in volume using the full power of the Linac Coherent Light Source (LCLS) and a dose up to 1.3 GGy per crystal. The crystalline shell of granulovirus OBs consists, on average, of about 9,000 unit cells, representing the smallest protein crystals to yield a high-resolution structure by X-ray crystallography to date. The XFEL structure shows little to no evidence of radiation damage and is more complete than a model determined using synchrotron data from recombinantly produced, much larger, cryocooled granulovirus granulin microcrystals. Our measurements suggest that it should be possible, under ideal experimental conditions, to obtain data from protein crystals with only 100 unit cells in volume using currently available XFELs and suggest that single-molecule imaging of individual biomolecules could almost be within reach.
关键词	XFEL nanocrystals structural biology bioimaging SFX
收录类别	SCI
语种	英语
资助项目	US Department of Energy, Office of Science, Office of Basic Energy Sciences[DE-AC02-76SF00515]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000395101200053
出版者	NATL ACAD SCIENCES
WOS关键词	RADIATION-DAMAGE ; STRUCTURE REFINEMENT ; DIFFRACTION ; CRYSTALS ; PHENIX ; MODEL
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1497
专题	iHuman研究所_公共科研平台_同步辐射线站 iHuman研究所_科学装置(X)_膜蛋白同步辐射线站
通讯作者	Metcalf, Peter; Chapman, Henry N.
作者单位	1.Ctr Free Elect Laser Sci, Deutsch Elektronen Synchrotron DESY, D-22607 Hamburg, Germany 2.Univ Auckland, Sch Biol Sci, Auckland 1142, New Zealand 3.European XFEL GmbH, D-22761 Hamburg, Germany 4.Arizona State Univ, Sch Mol Sci, Tempe, AZ 85287 USA 5.Arizona State Univ, Biodesign Ctr Appl Struct Discovery, Tempe, AZ 85287 USA 6.Max Planck Inst Med Res, Dept Biomol Mech, D-69120 Heidelberg, Germany 7.SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA 94025 USA 8.SLAC Natl Accelerator Lab, Menlo Pk, CA 94025 USA 9.Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA 10.Univ Basel, Ctr Cellular Imaging & NanoAnalyt CCINA, Biozentrum, CH-4058 Basel, Switzerland 11.Julius Kuehn Inst JKI, Inst Biol Control, D-64287 Darmstadt, Germany 12.Univ Hamburg, Dept Phys, D-20355 Hamburg, Germany 13.Univ Hamburg, Ctr Ultrafast Imaging, D-20355 Hamburg, Germany 14.MRC Lab Mol Biol, Cambridge CB2 OQH, England 15.Friedrich Miescher Inst Biomed Res, CH-4058 Basel, Switzerland 16.Paul Scherrer Inst, Swiss Light Source, CH-5232 Villigen, Switzerland 17.Univ Hamburg, Inst Biochem & Mol Biol, D-20146 Hamburg, Germany 18.Univ Wisconsin Milwaukee, Dept Phys, Milwaukee, WI 53211 USA 19.Natl Sci Fdn, BioXFEL Sci & Technol Ctr, Buffalo, NY 14203 USA 20.Paul Scherrer Inst, SwissFEL, CH-5232 Villigen, Switzerland 21.Shanghai Tech Univ, iHuman Inst, Shanghai 201210, Peoples R China 22.Brookhaven Natl Lab, NSLS II, Upton, NY 11973 USA
推荐引用方式 GB/T 7714	Gati, Cornelius,Oberthuer, Dominik,Yefanov, Oleksandr,et al. Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2017,114(9):2247-2252.
APA	Gati, Cornelius.,Oberthuer, Dominik.,Yefanov, Oleksandr.,Bunker, Richard D..,Stellato, Francesco.,...&Chapman, Henry N..(2017).Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,114(9),2247-2252.
MLA	Gati, Cornelius,et al."Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 114.9(2017):2247-2252.