Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 29, Issue -, Pages 1141-1151Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600577522007895
Keywords
fixed-target serial synchrotron crystallography; X-ray free-electron lasers; structural biology
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Funding
- National Institute of Allergy and Infectious Diseases, National Institutes of Health, Department of Health and Human Services [HHSN272201200026C, HHSN272201700060C]
- US Department of Energy (DOE) Office of Science
- DOE Office of Science [DE-AC02-06CH11357]
- US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
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Serial synchrotron crystallography is a method for studying protein structures using data collected from thousands of crystals at physiological temperature and reduced radiation damage. The Structural Biology Center used a new 3D-printed mesh-holder approach to optimize sample handling. By applying this system, two types of β-lactamases were successfully studied.
Serial synchrotron crystallography enables the study of protein structures under physiological temperature and reduced radiation damage by collection of data from thousands of crystals. The Structural Biology Center at Sector 19 of the Advanced Photon Source has implemented a fixed-target approach with a new 3D-printed mesh-holder optimized for sample handling. The holder immobilizes a crystal suspension or droplet emulsion on a nylon mesh, trapping and sealing a near-monolayer of crystals in its mother liquor between two thin Mylar films. Data can be rapidly collected in scan mode and analyzed in near real-time using piezoelectric linear stages assembled in an XYZ arrangement, controlled with a graphical user interface and analyzed using a high-performance computing pipeline. Here, the system was applied to two beta-lactamases: a class D serine beta-lactamase from Chitinophaga pinensis DSM 2588 and L1 metallo-beta-lactamase from Stenotrophomonas maltophilia K279a.
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