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首页> 外文期刊>Crystallography reports >Crystallization and Preliminary X-Ray Diffraction Study of Recombinant Ribokinase from Thermus Species 2.9
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Crystallization and Preliminary X-Ray Diffraction Study of Recombinant Ribokinase from Thermus Species 2.9

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摘要

Ribokinase from a thermophilic strain of Thermus species 2.9 belonging to the carbohydrate ribokinase family (EC 2.7.1.15) was isolated, purified, and crystallized. The crystallization conditions were found by the vapor-diffusion technique and were then optimized to apply the capillary counter-diffusion technique. The X-ray diffraction data set was collected from the crystals, which were grown by the counter-diffusion technique, at the SPring-8 synchrotron radiation facility to 2.87 angstrom resolution. The crystals belong to sp. gr. P1211 and have the following unit-cell parameters: a = 81.613 angstrom, b = 156.132 angstrom, c = 87.714 angstrom, alpha = gamma = 90 degrees, beta = 103.819 degrees. The X-ray diffraction data set is suitable for determining the three-dimensional structure of the protein by the molecular-replacement method.

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