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Preparation, Crystallization, and Preliminary X-Ray Diffraction Study of Mutant Carboxypeptidase T Bearing the Primary Specificity Pocket and the Active-Site Loop of Carboxypeptidase B
Crystallography Reports ( IF 0.6 ) Pub Date : 2020-11-20 , DOI: 10.1134/s106377452006005x
V. Kh. Akparov , G. E. Konstantinova , V. I. Timofeev , I. P. Kuranova , I. G. Khaliullin

Abstract

Crystals of mutant carboxypeptidase T from Thermoactinomyces vulgaris (CPT11QG) with amino-acid substitutions G215S, Q249G, A251G, T257A, D260G, T262D, and L254I and with the insertion ins253T were grown in microgravity by the capillary counter-diffusion method. The crystals belong to sp. gr. P31, which differs from the space group of the wild-type enzyme (P6322). The X-ray diffraction data set was collected from the crystals at the SPring-8 synchrotron facility (Japan) and is suitable for crystal structure determination at 2.45 Å resolution.



中文翻译:

带有羧肽酶B主要特异性口袋和活性位点环的突变型羧肽酶T的制备,结晶和X射线衍射初步研究

摘要

通过毛细管反扩散法在微重力下生长具有氨基酸取代基G215S,Q249G,A251G,T257A,D260G,T262D和L254I的寻常型嗜热放线菌(CPT11QG)突变型羧肽酶T的晶体。晶体属于sp。gr。 P 31,不同于野生型酶的空间群(P 6322)。X射线衍射数据集是从日本SPring-8同步加速器设施的晶体中收集的,适合于以2.45Å分辨率进行晶体结构测定。

更新日期:2020-11-21
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