铁肠杆菌素受体FepA（一种来自大肠杆菌的整合膜蛋白）的结晶及X射线初步分析

Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein from Escherichia coli.

作者信息

Smith B S, Kobe B, Kurumbail R, Buchanan S K, Venkatramani L, Van Der Helm D, Deisenhofer J

机构信息

Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Blvd, Dallas, Texas 75235-9050, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):697-9. doi: 10.1107/s0907444997020222.

DOI:10.1107/s0907444997020222

PMID:9761879

Abstract

Diffraction-quality crystals have been obtained of the integral membrane protein ferric enterobactin receptor (FepA) from the outer membrane of Escherichia coli. Crystals were grown using the zwitterionic detergent lauryldimethylamine oxide (LDAO), the precipitants polyethylene glycol (PEG) 1000 and sodium chloride, and the additive heptane-1,2,3-triol; they have the symmetry of the orthorhomic space group C2221 with a = 112.2, b = 137.2 and c = 135. 4 A and diffract to 2.5 A resolution. The crystals were flash-cooled and a preliminary data set was collected at 103 K. The crystals are suitable for three-dimensional structure analysis.

摘要

已获得来自大肠杆菌外膜的完整膜蛋白铁肠杆菌素受体（FepA）的衍射质量晶体。使用两性离子去污剂月桂基二甲基氧化胺（LDAO）、沉淀剂聚乙二醇（PEG）1000和氯化钠以及添加剂庚烷-1,2,3-三醇培养晶体；它们具有正交空间群C2221的对称性，a = 112.2，b = 137.2，c = 135.4 Å，并且衍射到2.5 Å分辨率。晶体经快速冷却，并在103 K下收集了初步数据集。这些晶体适用于三维结构分析。