Open AccessExpression, crystallization and preliminary X‐ray analysis of an outer membrane protein from Thermus thermophilus HB27
Author(s) -
Brosig Alexander,
Nesper Jutta,
Welte Wolfram,
Diederichs Kay
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108013602
Subject(s) - thermus thermophilus , bacterial outer membrane , membrane , cell envelope , thermophile , biology , escherichia coli , crystallography , membrane protein , crystallization , bacteria , biophysics , chemistry , biochemistry , gene , genetics , organic chemistry
The cell envelope of the thermophilic bacterium Thermus thermophilus is multilayered and includes an outer membrane with integral outer membrane proteins that are not well characterized. The hypothetical protein TTC0834 from T. thermophilus HB27 was identified as a 22 kDa outer membrane protein containing eight predicted β‐strands. TTC0834 was expressed with an N‐terminal His tag in T. thermophilus HB8 and detected in the S‐layer/outer membrane envelope fraction. His‐TTC0834 was purified and crystallized under various conditions. Native data sets were collected to 3.2 Å resolution and the best diffracting crystals belonged to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 166.67, c = 97.53 Å.