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

Gati, Cornelius and Oberthuer, Dominik and Yefanov, Oleksandr and Bunker, Richard D. and Stellato, Francesco and Chiu, Elaine and Yeh, Shin-Mei and Aquila, Andrew and Basu, Shibom and Bean, Richard and Beyerlein, Kenneth R. and Botha, Sabine and Boutet, Sébastien and DePonte, Daniel P. and Doak, R. Bruce and Fromme, Raimund and Galli, Lorenzo and Grotjohann, Ingo and James, Daniel R. and Kupitz, Christopher and Lomb, Lukas and Messerschmidt, Marc and Nass, Karol and Rendek, Kimberly and Shoeman, Robert L. and Wang, Dingjie and Weierstall, Uwe and White, Thomas A. and Williams, Garth J. and Zatsepin, Nadia A. and Fromme, Petra and Spence, John C. H. and Goldie, Kenneth N. and Jehle, Johannes A. and Metcalf, Peter and Barty, Anton and 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). pp. 2247-2252.

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Official URL: https://edoc.unibas.ch/78546/

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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 from X-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 μm3 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 Å resolution structure of native nanocrystalline granulovirus occlusion bodies (OBs) that are less than 0.016 μm3 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.
Faculties and Departments:05 Faculty of Science
UniBasel Contributors:Goldie, Kenneth N.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:National Academy of Sciences
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:01 Oct 2020 08:59
Deposited On:01 Oct 2020 08:59

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