Bibliographic Details
Title: |
Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
Authors: |
Cecilia M. Casadei, Karol Nass, Anton Barty, Mark S. Hunter, Celestino Padeste, Ching-Ju Tsai, Sébastien Boutet, Marc Messerschmidt, Leonardo Sala, Garth J. Williams, Dmitry Ozerov, Matthew Coleman, Xiao-Dan Li, Matthias Frank, Bill Pedrini |
Source: |
IUCrJ, Vol 6, Iss 1, Pp 34-45 (2019) |
Publisher Information: |
International Union of Crystallography, 2019. |
Publication Year: |
2019 |
Collection: |
LCC:Crystallography |
Subject Terms: |
free-electron lasers, serial femtosecond crystallography, membrane proteins, two-dimensional crystals, Crystallography, QD901-999 |
More Details: |
Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments. |
Document Type: |
article |
File Description: |
electronic resource |
Language: |
English |
ISSN: |
2052-2525 20522525 |
Relation: |
http://scripts.iucr.org/cgi-bin/paper?S2052252518014641; https://doaj.org/toc/2052-2525 |
DOI: |
10.1107/S2052252518014641 |
Access URL: |
https://doaj.org/article/1a712444222c42ae9abe2b27756b4020 |
Accession Number: |
edsdoj.1a712444222c42ae9abe2b27756b4020 |
Database: |
Directory of Open Access Journals |