Image reconstruction in serial femtosecond nanocrystallography using x-ray free-electron lasers

Joe P. J. Chen; Richard A. Kirian; Kenneth R. Beyerlein; Richard J. Bean; Andrew J. Morgan; Oleksandr M. Yefanov; Romain D. Arnal; David H. Wojtas; Phil J. Bones; Henry N. Chapman; John C. H. Spence; Rick P. Millane

doi:10.1117/12.2187610

21 September 2015 Image reconstruction in serial femtosecond nanocrystallography using x-ray free-electron lasers

Joe P. J. Chen, Richard A. Kirian, Kenneth R. Beyerlein, Richard J. Bean, Andrew J. Morgan, Oleksandr M. Yefanov, Romain D. Arnal, David H. Wojtas, Phil J. Bones, Henry N. Chapman, John C. H. Spence, Rick P. Millane

Author Affiliations +

Proceedings Volume 9600, Image Reconstruction from Incomplete Data VIII; 960002 (2015) https://doi.org/10.1117/12.2187610
Event: SPIE Optical Engineering + Applications, 2015, San Diego, California, United States

Abstract

Serial femtosecond nanocrystallography (SFX) is a form of x-ray coherent diffraction imaging that utilises a stream of tiny nanocrystals of the biological assembly under study, in contrast to the larger crystals used in conventional x-ray crystallography using conventional x-ray synchrotron x-ray sources. Nanocrystallography utilises the extremely brief and intense x-ray pulses that are obtained from an x-ray free-electron laser (XFEL). A key advantage is that some biological macromolecules, such as membrane proteins for example, do not easily form large crystals, but spontaneously form nanocrystals. There is therefore an opportunity for structure determination for biological molecules that are inaccessible using conventional x-ray crystallography. Nanocrystallography introduces a number of interesting image reconstruction problems. Weak diffraction patterns are recorded from hundreds of thousands of nancocrystals in unknown orientations, and these data have to be assembled and merged into a 3D intensity dataset. The diffracted intensities can also be affected by the surface structure of the crystals that can contain incomplete unit cells. Furthermore, the small crystal size means that there is potentially access to diffraction information between the crystalline Bragg peaks. With this information, phase retrieval is possible without resorting to the collection of additional experimental data as is necessary in conventional protein crystallography. We report recent work on the diffraction characteristics of nanocrystals and the resulting reconstruction algorithms.

Citation Download Citation

Joe P. J. Chen, Richard A. Kirian, Kenneth R. Beyerlein, Richard J. Bean, Andrew J. Morgan, Oleksandr M. Yefanov, Romain D. Arnal, David H. Wojtas, Phil J. Bones, Henry N. Chapman, John C. H. Spence, and Rick P. Millane "Image reconstruction in serial femtosecond nanocrystallography using x-ray free-electron lasers", Proc. SPIE 9600, Image Reconstruction from Incomplete Data VIII, 960002 (21 September 2015); https://doi.org/10.1117/12.2187610

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available