Expression, crystallization and preliminary X-ray analysis of an outer membrane protein from Thermus thermophilus HB27.
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 beta-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 A resolution and the best diffracting crystals belonged to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 166.67, c = 97.53 A.
Brosig
Alexander
A
Department of Biology, University of Konstanz, 78457 Konstanz, Germany.
Nesper
Jutta
J
Welte
Wolfram
W
Diederichs
Kay
K
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D005798:Genes, Bacterial; D006639:Histidine / Q000737:chemistry; D008970:Molecular Weight; D021141:Nucleic Acid Amplification Techniques; D017433:Protein Structure, Secondary; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D001425:Bacterial Outer Membrane Proteins; D006639:Histidine