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Overproduction, crystallization and preliminary X‐ray crystallographic analysis of Escherichia coli tRNA N 6 ‐threonylcarbamoyladenosine dehydratase
Author(s) -
Kim Sunmin,
Kim Keon Young,
Park Jeong Kuk,
Lee Byung Il,
Kim YunGon,
Park SangYoun
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14020883
Subject(s) - crystallization , dehydratase , crystallography , escherichia coli , transfer rna , polyethylene glycol , x ray crystallography , monomer , resolution (logic) , chemistry , x ray , crystal structure , crystal (programming language) , diffraction , physics , rna , enzyme , biochemistry , optics , organic chemistry , artificial intelligence , computer science , gene , polymer , programming language
Escherichia coli tRNA N 6 ‐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 P 2 1 , 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 ( V M ) of 2.12 Å 3 Da −1 and 42.1% solvent content.