Open AccessAnti‐TRAP protein from Bacillus subtilis : crystallization and internal symmetry
Author(s) -
Shevtsov Mikhail B.,
Chen Yanling,
Gollnick Paul,
Antson Alfred A.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904011199
Subject(s) - bacillus subtilis , crystallization , trimer , dodecameric protein , crystallography , chemistry , trap (plumbing) , symmetry (geometry) , physics , biology , dna , biochemistry , dimer , organic chemistry , geometry , genetics , mathematics , meteorology , bacteria
Anti‐TRAP protein regulates the expression of tryptophan biosynthetic genes by binding to TRAP and preventing formation of the TRAP–RNA complex. Anti‐TRAP from Bacillus subtilis has been crystallized by vapour diffusion. The crystals belong to space group P 1, with unit‐cell parameters a = 51.6, b = 60.1, c = 60.4 Å, α = 114.0, β = 101.4, γ = 100.5°. X‐ray data have been collected to 2.8 Å resolution. Peaks in the self‐rotation function correspond to four trimers in the unit cell related by twofold and threefold rotational axes. The symmetry and gel‐filtration data suggest that the protein exists as a trimer or a dodecamer in solution.