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- Title
Crystallization and Preliminary X-Ray Diffraction Analysis of Recombinant Phosphoribosylpyrophosphate Synthetase I from Thermus thermophilus HB27.
- Authors
Abramchik, Yu. A.; Timofeev, V. I.; Zhukhlistova, N. E.; Shevtsov, M. B.; Fateev, I. V.; Kostromina, M. A.; Zayats, E. A.; Kuranova, I. P.; Esipov, R. S.
- Abstract
Crystals of phosphoribosylpyrophosphate synthetase from the thermophilic bacterium Thermus thermophilus (Tth PRPPS1 HB27), suitable for X-ray diffraction, were grown by the hanging-drop vapor-diffusion method. Before X-ray diffraction data collection, the crystals were transferred to a cryoprotectant solution and were flash-frozen in liquid nitrogen stream. These crystals were used to collect the X-ray diffraction data set on the European Synchrotron Radiation Facility (ESRF, France, ID23-1 beamline) at 100 K to 2.6 Å resolution, which was suitable for determining the three-dimensional structure of the enzyme.
- Subjects
FRANCE; THERMUS thermophilus; X-ray diffraction; THERMOPHILIC bacteria; SYNCHROTRON radiation; CRYSTALLIZATION
- Publication
Crystallography Reports, 2022, Vol 67, Issue 4, p586
- ISSN
1063-7745
- Publication type
Article
- DOI
10.1134/S1063774522040022