Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8.

Vassylyeva MN; Sakai H; Matsuura TSekine SINishiyama MTerada TShirouzu MKuramitsu SVassylyev DGYokoyama S

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8.

【24h】

Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8.

机译：克隆、表达、纯化、结晶和初始晶体的分析lysine-biosynthesis LysX蛋白质从栖热菌属酸奶有助于HB8。

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

The gene encoding LysX, an essential component of the lysine-biosynthesis pathway in Thermus thermophilus (molecular weight approximately 31 000 Da), was cloned and expressed and the purified protein was crystallized by the hanging-drop vapour-diffusion technique in two different space groups, C2 (unit-cell parameters a = 124.7, b = 51.4, c = 103.6 A, beta = 122.8 degrees ) and R3 (a = b = 122.6, c = 97.6 A). Crystals improved by macroseeding diffracted to beyond 2.3 and 3 A resolution for the C2 and R3 crystal forms, respectively. Complete diffraction data sets were collected for the C2 and R3 crystal forms at 2.5 and 3.1 A resolution, respectively. Crystals of selenomethionine-containing LysX protein were obtained by cross-microseeding, using the native microcrystals as a seed. Structure determination is now in progress.

机译：该基因编码LysX,一个重要的组成部分在栖热菌属lysine-biosynthesis通路酸奶(分子量约为31000 Da),克隆和表达纯化蛋白质结晶了在两个悬滴vapour-diffusion技术不同的空间组织,C2(晶胞参数b = 51.4 = 124.7, c = 103.6,β= 122.8度)和R3 (a = b = 122.6, c = 97.6)。提高了macroseeding晶体衍射超出2.3和3 C2和R3的决议水晶形式,分别。数据集收集C2和R3晶体形式在2.5和3.1的决议,分别。selenomethionine-containing LysX蛋白质是通过cross-microseeding,使用本机作为种子微晶核。现在在进步。

著录项

来源
《Acta crystallographica.Section D. Biological crystallography》 |2003年第9期|1651-1652|共2页
作者
Vassylyeva MN; Sakai H; Matsuura TSekine SINishiyama MTerada TShirouzu MKuramitsu SVassylyev DGYokoyama S;
展开▼
作者单位

Genomic Sciences Center, RIKEN Yokohama Institute, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, and Structurome Project, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan.;

展开▼
收录信息
原文格式 PDF
正文语种英语
中图分类化学;
关键词
Thermus thermophilus; crystals; Macrophage-1 AntigenAnabolismLysineCrystallization;

机译：栖热菌属酸奶;晶体;Macrophage-1AntigenAnabolismLysineCrystallization;

相似文献

外文文献
中文文献

1. Prokaryotic Expression, Purification, Antibody Production of a NH2-Terminal Fragment of mCLCA3 Protein and Analysis of mClCA3 Protein Expression in Asthmatic Mouse Lung [J] . HOU Xia, WU Qing-tian, ZHANG Yu-ping, 高等学校化学研究（英文版） . 2007,第006期
2. Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein [O] . Chen I.J., Chou C.C., Liu C.L., 2014

机译：Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein

Cloning, expression, purification, crystallization and initial crystallographic analysis of the lysine-biosynthesis LysX protein from Thermus thermophilus HB8.

摘要

著录项

相似文献

相关主题

期刊订阅