Crystallization of OmpC osmoporin from Escherichia coli

被引：5

作者：

Kim, H ^{[1
]}

机构：

[1] Univ Texas, SW Med Ctr, Dallas, TX 75235 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444998004570

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

OmpC porin, one of the major outer-membrane proteins of Cram-negative bacteria, participates in bacterial osmoregulation by counteracting OmpF porin. Although these two osmoporins from Escherichia coli share high sequence homology, their crystallization behavior was found to be very different. OmpC could be crystallized under a variety of conditions by either microdialysis or hanging-drop methods using PEG 4000 as precipitant. The crystals belong to space group P2(1) with unit-cell constants a = 117.6, b -110, c = 298.4 Angstrom, beta = 97 degrees. They diffract beyond 4 Angstrom with a rotating anode and show intense non-Bragg scattering.

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页码：1399 / 1400

页数：2

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