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Overproduction, crystallization and preliminary X-ray crystallographic analysis of Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase.

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 P2?, with unit-cell parameters a=65.4, b=96.8, c=83.3?Å, ?=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.

SUBMITTER: Kim S

PROVIDER: S-EPMC4231855 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Overproduction, crystallization and preliminary X-ray crystallographic analysis of Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase.

Kim Sunmin S Kim Keon Young KY Park Jeong Kuk JK Lee Byung Il BI Kim Yun-Gon YG Park SangYoun S

Acta crystallographica. Section F, Structural biology communications 20141025 Pt 11

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 contai ...[more]

PMID: 25372820

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