CRYSTALLIZATION AND PRELIMINARY-X-RAY CHARACTERIZATION OF MALTOPORIN FROM ESCHERICHIA-COLI

被引：31

作者：

STAUFFER, KA

PAGE, MGP

HARDMEYER, A

KELLER, TA

PAUPTIT, RA

机构：

[1] UNIV BASEL,DEPT MICROBIOL,CH-4056 BASEL,SWITZERLAND

[2] UNIV BASEL,BIOCTR,DEPT STRUCT BIOL,CH-4056 BASEL,SWITZERLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 211卷 / 02期

关键词：

D O I：

10.1016/0022-2836(90)90351-L

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Crystals of maltoporin (the bacteriophage λ receptor of Escherichia coli) that diffract X-rays to 3 Å 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 C2221 with unit cell dimensions a = 130 A ̊,b = 213 A ̊ and c = 216 A ̊. X-ray structure determination is underway. © 1990.

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页码：297 / 299

页数：3

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