大肠杆菌麦芽糖孔蛋白的结晶及X射线初步表征

Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli.

作者信息

Stauffer K A, Page M G, Hardmeyer A, Keller T A, Pauptit R A

机构信息

Department of Microbiology, University of Basel, Switzerland.

出版信息

J Mol Biol. 1990 Jan 20;211(2):297-9. doi: 10.1016/0022-2836(90)90351-L.

DOI:10.1016/0022-2836(90)90351-L

PMID:2137884

Abstract

Crystals of maltoporin (the bacteriophage lambda receptor of Escherichia coli) that diffract X-rays to 3 A resolution can be grown reproducibly. Maltoporin is an integral membrane protein, which forms a channel in the E. coli outer membrane that specifically facilitates the diffusion of maltose and maltodextrins. The crystals have a rhombic prismatic habit and belong to the orthorhombic space group C222(1) with unit cell dimensions a = 130 A, b = 213 A and c = 216 A. X-ray structure determination is underway.

摘要

可以重复性地生长出能将X射线衍射到3埃分辨率的麦芽寡糖孔蛋白（大肠杆菌的噬菌体λ受体）晶体。麦芽寡糖孔蛋白是一种整合膜蛋白，它在大肠杆菌外膜中形成一个通道，专门促进麦芽糖和麦芽糊精的扩散。这些晶体呈菱形棱柱习性，属于正交空间群C222(1)，晶胞尺寸为a = 130埃，b = 213埃，c = 216埃。X射线结构测定正在进行中。