Cryst. Rep, 2022, 67(4):pages 586–589

Crystallization and Preliminary X-Ray Diffraction Analysis of Recombinant Phosphoribosylpyrophosphate Synthetase I from Thermus thermophilus HB27

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.

Abramchik YA, Timofeev VI, Zhukhlistova NE, Shevtsov MB, Fateev IV, Kostromina MA, Zayats EA, Kuranova IP, Esipov RS

IBCH: 10360
Ссылка на статью в журнале: https://link.springer.com/article/10.1134/S1063774522040022
Кол-во цитирований на 10.2024: 0
Данные статьи проверены модераторами 2022-12-08

Список научных проектов, где отмечена публикация

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