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枯草芽孢杆菌含组氨酸的磷酸载体蛋白HPr及其一些定点突变体的结晶。

Crystallization of the Bacillus subtilis histidine-containing phosphocarrier protein HPr and of some of its site-directed mutants.

作者信息

Kapadia G, Reizer J, Sutrina S L, Saier M H, Reddy P, Herzberg O

机构信息

Center for Advanced Research in Biotechnology, University of Maryland, Rockville 20850.

出版信息

J Mol Biol. 1990 Mar 5;212(1):1-2. doi: 10.1016/0022-2836(90)90296-X.

Abstract

The histidine-containing phosphocarrier protein (HPr) from Bacillus subtilis has been crystallized. Two of the site-directed mutants aimed at probing function produce crystals suitable for X-ray studies. The mutant in which His15 is substituted by an alanyl residue crystallizes from ammonium sulfate solution in space group P3(1)21 or P3(2)21, with unit cell dimensions: a = b = 47.3 A; c = 61.5 A. These crystals diffract to at least 1.8 A resolution. The mutant in which Ser46 is substituted by an aspartyl residue crystallizes from polyethylene glycol 4000 solution in space group P2(1), with unit cell dimensions: a = 49.4 A; b = 25.6 A; c = 60.3 A; beta = 109 degrees. These crystals diffract to at least 2.0 A resolution.

摘要

来自枯草芽孢杆菌的含组氨酸磷酸载体蛋白(HPr)已被结晶。旨在探究功能的两个定点突变体产生了适合X射线研究的晶体。His15被丙氨酰残基取代的突变体从硫酸铵溶液中结晶,空间群为P3(1)21或P3(2)21,晶胞参数为:a = b = 47.3 Å;c = 61.5 Å。这些晶体的衍射分辨率至少为1.8 Å。Ser46被天冬氨酰残基取代的突变体从聚乙二醇4000溶液中结晶,空间群为P2(1),晶胞参数为:a = 49.4 Å;b = 25.6 Å;c = 60.3 Å;β = 109°。这些晶体的衍射分辨率至少为2.0 Å。

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