| Literature DB >> 25372820 |
Sunmin Kim1, Keon Young Kim1, Jeong Kuk Park1, Byung Il Lee2, Yun-Gon Kim3, SangYoun Park1.
Abstract
Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase (TcdA), previously called CsdL or YgdL, was overproduced and purified from E. coli and crystallized using polyethylene glycol 3350 as a crystallizing agent. X-ray diffraction data were collected to 2.70 Å resolution under cryoconditions using synchrotron X-rays. The crystals belonged to space group P2₁, with unit-cell parameters a=65.4, b=96.8, c=83.3 Å, β=111.7°. According to the Matthews coefficient, the asymmetric unit may contain up to four subunits of the monomeric protein, with a crystal volume per protein mass (VM) of 2.12 Å3 Da(-1) and 42.1% solvent content.Entities:
Keywords: CsdL; N6-threonylcarbamoyladenosine dehydratase; TcdA; tRNA hypermodification
Mesh:
Substances:
Year: 2014 PMID: 25372820 PMCID: PMC4231855 DOI: 10.1107/S2053230X14020883
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056