Journal
JOURNAL OF APPLIED CRYSTALLOGRAPHY
Volume 48, Issue -, Pages 1072-1079Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600576715010493
Keywords
X-ray free-electron lasers; biological crystallography; two-dimensional crystallography; microcrystallography; serial femtosecond crystallography
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Funding
- US Department of Energy [DE-AC52-07NA27344]
- Pacific Northwest National Laboratory [DE-AC05-76RL01830]
- LLNL Lab-Directed Research and Development (LDRD) Project [12-ERD-031]
- PNNL Chemical Imaging Initiative
- NSF Brandeis MRSEC [DMR-0820492]
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X-ray free-electron lasers (XFELs) offer a new avenue to the structural probing of complex materials, including biomolecules. Delivery of precious sample to the XFEL beam is a key consideration, as the sample of interest must be serially replaced after each destructive pulse. The fixed-target approach to sample delivery involves depositing samples on a thin-film support and subsequent serial introduction via a translating stage. Some classes of biological materials, including two-dimensional protein crystals, must be introduced on fixed-target supports, as they require a flat surface to prevent sample wrinkling. A series of wafer and transmission electron microscopy (TEM)-style grid supports constructed of low-Z plastic have been custom-designed and produced. Aluminium TEM grid holders were engineered, capable of delivering up to 20 different conventional or plastic TEM grids using fixed-target stages available at the Linac Coherent Light Source (LCLS). As proof-of-principle, X-ray diffraction has been demonstrated from two-dimensional crystals of bacteriorhodopsin and three-dimensional crystals of anthrax toxin protective antigen mounted on these supports at the LCLS. The benefits and limitations of these low-Z fixed-target supports are discussed; it is the authors' belief that they represent a viable and efficient alternative to previously reported fixed-target supports for conducting diffraction studies with XFELs.
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