来自博来霉素产生菌轮枝链霉菌的博来霉素结合蛋白的结晶及初步X射线衍射研究。

Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus.

作者信息

Kumagai T, Muta K, Matoba Y, Kawano Y, Kamiya N, Davies J, Sugiyama M

机构信息

Institute of Pharmaceutical Sciences, Hiroshima University School of Medicine, Kasumi 1-2-3, Minami-ku, Hiroshima 734, Japan.

出版信息

Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):127-8. doi: 10.1107/s0907444997008871.

DOI:10.1107/s0907444997008871

PMID:9761833

Abstract

A bleomycin-binding protein (BLMA) produced by bleomycin-producing Streptomyces verticullus was crystallized in a form suitable for X-ray diffraction analysis using the vapor-diffusion method. Crystals were grown at pH 5.7, in 0.2 M NH4 actate and 0.1 M Na acetate, using 30% PEG 4000 as a precipitant. They belong to the orthorhombic system, with space group P21212, cell dimensions a = 54. 90, b = 67.94, c = 35.60 A, and one BLMA molecule in the asymmetric unit. The crystals diffract X-rays well and the diffraction intensity data was collected up to 1.5 A resolution with a merging R value of 0.054 at beamline 6B of the Photon Factory. The diffraction data set is 94% complete.

摘要

由产博来霉素的轮状链霉菌产生的一种博来霉素结合蛋白（BLMA），采用气相扩散法结晶为适合X射线衍射分析的形式。晶体在pH 5.7、0.2M醋酸铵和0.1M醋酸钠中生长，使用30%聚乙二醇4000作为沉淀剂。它们属于正交晶系，空间群为P21212，晶胞参数a = 54.90，b = 67.94，c = 35.60 Å，不对称单元中有一个BLMA分子。这些晶体对X射线衍射良好，在光子工厂6B束线收集了分辨率高达1.5 Å的衍射强度数据，合并R值为0.054。衍射数据集的完整性为94%。