The recent development of X-ray free electron lasers (XFELs) has spurred the development of serial femtosecond nanocrystallography (SFX) which, for the first time, is enabling structure retrieval from sub-micron protein crystals. Although there are already a growing number of structures published using SFX, the technology is still very new and presents a number of unique challenges as well as opportunities for structural biologists. One of the biggest barriers to the success of SFX experiments is the preparation and selection of suitable protein crystal samples. Here we outline a protocol for preparing and screening for suitable XFEL targets.
Funding
Part of this research was undertaken on the MX2 beamlines at the Australian Synchrotron, Victoria, Australia. The work was carried out in collaboration with the ARC Centre of Excellence in Advanced Molecular Imaging (CE140100011) www.imagingcoe.org. The research has been supported by the National Health and Medical Research Council (NHMRC) Program (1000512, 565526), Project (1003326, 1107804) and Research Fellowship (1003325, 1110971) to BK.
History
Publication Date
2016-05-03
Journal
Scientific Reports
Volume
6
Issue
1
Article Number
25345
Pagination
8p.
Publisher
Springer Nature
ISSN
2045-2322
Rights Statement
This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/