Crystallization and preliminary X-ray investigation of the complex of RNase Sa with wild-type barstar

被引：4
|
作者：
Urbanikova, L [1 ]
Sevcik, J [1 ]
机构：
[1] Slovak Acad Sci, Inst Mol Biol, Bratislava 84251, Slovakia
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷
关键词：
D O I：
10.1107/S0907444997010688
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
RNase Sa, an extracellular ribonuclease produced by Streptomyces aureofaciens, is inhibited by barstar, the natural protein inhibitor of barnase, the ribonuclease of Bacillus amyloliquefaciens. The complex of RNase Sa with wild-type barstar was crystallized by hanging-drop vapour diffusion. It was shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis that RNase Sa and barstar are present in equimolar proportions in the crystals. The crystals are in the hexagonal space group P6(5) with unit-cell dimensions a = b = 56.95, c = 135.8 Angstrom. They diffract to 1.7 Angstrom resolution at the DESY synchrotron source. The asymmetric unit contains one molecule of the complex.
引用
收藏
页码：403 / 404
页数：2
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