Isolation, purification, crystallization, and preliminary X-ray diffraction study of the crystals of HU protein from M-gallisepticum

被引：10

作者：

Nikolaeva, A. Yu. ^{[1
,2
]}

Timofeev, V. I. ^{[1
,3
]}

Boiko, K. M. ^{[1
,2
]}

Korzhenevskii, D. A. ^{[1
]}

Rakitina, T. V. ^{[1
,4
]}

Dorovatovskii, P. V. ^{[1
]}

Lipkin, A. V. ^{[1
,2
]}

机构：

[1] Kurchatov Inst, Natl Res Ctr, Moscow 123098, Russia

[2] Russian Acad Sci, AN Bakh Biochem Inst, Biotechnol Res Ctr, Moscow 119071, Russia

[3] Russian Acad Sci, AV Shubnikov Crystallog Inst, Moscow 119333, Russia

[4] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia

来源：

CRYSTALLOGRAPHY REPORTS | 2015年 / 60卷 / 06期

基金：

俄罗斯科学基金会;

关键词：

DNA-BINDING PROTEIN; HISTONE-LIKE PROTEINS; ESCHERICHIA-COLI; BACTERIA; EXPRESSION; REPAIR; GENOME; GENES;

D O I：

10.1134/S1063774515060231

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

HU proteins are involved in bacterial DNA and RNA repair. Since these proteins are absent in cells of higher organisms, inhibitors of HU proteins can be used as effective and safe antibiotics. The crystallization conditions for the M. gallisepticum HU protein were found and optimized by the vapor-diffusion method. The X-ray diffraction data set was collected to 2.91 resolution from the crystals grown by the vapor-diffusion method on a synchrotron source. The crystals of the HU protein belong to sp. gr. P4(1)2(1)2 and have the following unit-cell parameters: a = b = 97.94 , c = 77.92 , alpha = beta = gamma = 90 degrees.

引用

页码：880 / 883

页数：4

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