Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 68, Issue -, Pages 592-600Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444912006749
Keywords
in situ diffraction; microfocus; microbeams; high throughput; room temperature; viruses; membrane proteins; synchrotron radiation
Funding
- Wellcome Trust [062164/Z/00/Z]
- MRC
- BBSRC
- Arthritis Research UK [13569, 18066]
- National Institute for Health Research
- P-CUBE, EU [227764]
- Medical Research Council [G1100525, G1000099] Funding Source: researchfish
- Versus Arthritis [19764] Funding Source: researchfish
- MRC [G1000099] Funding Source: UKRI
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Despite significant progress in high-throughput methods in macromolecular crystallography, the production of diffraction-quality crystals remains a major bottleneck. By recording diffraction in situ from crystals in their crystallization plates at similar to room temperature, a number of problems associated with crystal handling and cryoprotection can be side-stepped. Using a dedicated goniometer installed on the microfocus macromolecular crystallography beamline I24 at Diamond Light Source, crystals have been studied in situ with an intense and flexible microfocus beam, allowing weakly diffracting samples to be assessed without a manual crystal-handling step but with good signal to noise, despite the background scatter from the plate. A number of case studies are reported: the structure solution of bovine enterovirus 2, crystallization screening of membrane proteins and complexes, and structure solution from crystallization hits produced via a high-throughput pipeline. These demonstrate the potential for in situ data collection and structure solution with microbeams.
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