Suppr超能文献

酵母磷酸化传递蛋白YPD1的纯化、结晶及初步X射线衍射分析

Purification, crystallization and preliminary X-ray diffraction analysis of the yeast phosphorelay protein YPD1.

作者信息

Xu Q, Nguyen V, West A H

机构信息

Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):291-3. doi: 10.1107/S090744499800866X. Epub 1999 Jan 1.

Abstract

YPD1 is a yeast osmoregulatory protein that functions in a phosphorelay signal-transduction pathway. YPD1 has been expressed in Escherichia coli, purified to homogeneity and crystallized. The crystals were obtained by hanging-drop vapor-diffusion using PEG 4000 as a precipitant. Preliminary X-ray diffraction analysis indicates that the crystals belong to tetragonal space group P43212 or P41212 with unit-cell dimensions a = b = 52.71, c = 244.02 A. X-ray data to 2.7 and 3.0 A have been collected from native crystals and a heavy-atom derivative, respectively. Positions for two Hg atoms have been located by analysis of difference Patterson maps.

摘要

YPD1是一种酵母渗透调节蛋白,在磷酸化信号转导途径中发挥作用。YPD1已在大肠杆菌中表达,纯化至同质并结晶。通过使用聚乙二醇4000作为沉淀剂的悬滴气相扩散法获得晶体。初步X射线衍射分析表明,晶体属于四方晶系空间群P43212或P41212,晶胞参数a = b = 52.71,c = 244.02 Å。分别从天然晶体和重原子衍生物收集了2.7 Å和3.0 Å的X射线数据。通过分析差值帕特森图确定了两个汞原子的位置。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验