Open AccessExpression, purification, crystallization and preliminary X‐ray studies of the TAN1 orthologue from Methanothermobacter thermautotrophicus
Author(s) -
Silva Ana P. G.,
Byrne Robert T.,
Chechik Maria,
Smits Callum,
Waterman David G.,
Antson Alfred A.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108034039
Subject(s) - crystallization , domain (mathematical analysis) , monomer , saccharomyces cerevisiae , chemistry , catalysis , crystallography , biology , stereochemistry , biochemistry , gene , polymer , organic chemistry , mathematical analysis , mathematics
MTH909 is the Methanothermobacter thermautotrophicus orthologue of Saccharomyces cerevisiae TAN1, which is required for N 4 ‐acetylcytidine formation in tRNA. The protein consists of an N‐terminal near‐ferredoxin‐like domain and a C‐terminal THUMP domain. Unlike most other proteins containing the THUMP domain, TAN1 lacks any catalytic domains and has been proposed to form a complex with a catalytic protein that is capable of making base modifications. MTH909 has been cloned, overexpressed and purified. The molecule exists as a monomer in solution. X‐ray data were collected to 2.85 Å resolution from a native crystal belonging to space group P 6 1 22 (or P 6 5 22), with unit‐cell parameters a = 69.9, c = 408.5 Å.