Crystallization of domains involved in self-assembly of the S-layer protein SbsC

被引：6
|
作者：
Dordic, Andela [1 ]
Egelseer, Eva M. [2 ]
Tesarz, Manfred [2 ]
Sleytr, Uwe B. [2 ]
Keller, Walter [1 ]
Pavkov-Keller, Tea [1 ,3 ]
机构：
[1] Karl Franzens Univ Graz, Inst Mol Biosci, A-8010 Graz, Austria
[2] Univ Nat Resources & Life Sci, Dept Nanobiotechnol, A-1190 Vienna, Austria
[3] ACIB Austrian Ctr Ind Biotechnol GmbH, A-8010 Graz, Austria
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2012年 / 68卷
基金：
奥地利科学基金会;
关键词：
SURFACE-LAYER; STEAROTHERMOPHILUS ATCC-12980; BACTERIAL;
D O I：
10.1107/S1744309112042650
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The Gram-positive bacterium Geobacillus stearothermophilus ATCC 12980 is completely covered with a two-dimensional crystalline monolayer composed of the S-layer protein SbsC. In order to complete the structure of the full-length protein, additional soluble constructs containing the crucial domains for self-assembly have been successfully cloned, expressed and purified. Crystals obtained from three different recombinant constructs yielded diffraction to 3.4, 2.8 and 1.5 angstrom resolution. Native data have been collected.
引用
收藏
页码：1511 / 1514
页数：4
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