Journal
IUCRJ
Volume 1, Issue -, Pages 87-94Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252513033939
Keywords
protein microcrystallography; serial crystallography; in vivo grown microcrystals
Funding
- PIER Graduate School, Helmholtz Association Scholarship
- German Federal Ministry for Education and Research (BMBF) [01KX0806, 01KX0807]
- BMBF [05K12GU3]
- Hamburg Ministry of Science and Research and Joachim Herz Stiftung, Hamburg Initiative for Excellence in Research (LEXI)
- Hamburg School for Structure and Dynamics (SDI)
- DFG Cluster of Excellence 'Inflammation at Interfaces' [EXC 306]
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Crystal structure determinations of biological macromolecules are limited by the availability of sufficiently sized crystals and by the fact that crystal quality deteriorates during data collection owing to radiation damage. Exploiting a micrometre-sized X-ray beam, high-precision diffractometry and shutterless data acquisition with a pixel-array detector, a strategy for collecting data from many micrometre-sized crystals presented to an X-ray beam in a vitrified suspension is demonstrated. By combining diffraction data from 80 Trypanosoma brucei procathepsin B crystals with an average volume of 9 mu m(3), a complete data set to 3.0 angstrom resolution has been assembled. The data allowed the refinement of a structural model that is consistent with that previously obtained using free-electron laser radiation, providing mutual validation. Further improvements of the serial synchrotron crystallography technique and its combination with serial femtosecond crystallography are discussed that may allow the determination of high-resolution structures of micrometre-sized crystals.
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