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Crystallization and preliminary X-ray diffraction analysis of a thermostable GDSL-family esterase, EstL5, from Geobacillus thermodenitrificans T2.

ABSTRACT: The novel thermostable esterase EstL5 belonging to the GDSL family exhibits a unique cold-adaptation feature at low temperatures. To better understand its biochemical and enzymatic properties, recombinant EstL5 protein was purified and crystallized using the vapour-diffusion method. The EstL5 crystals diffracted X-rays to 2.79 Å resolution using a synchrotron-radiation source, belonged to the tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 101.51, c = 124.22 Å, and are expected to contain two molecules in each asymmetric unit. To obtain initial phases, selenomethionyl-substituted protein was overproduced. Purified SeMet-labelled EstL5 protein was crystallized and formed crystals that diffracted to a resolution of 3.0 Å.

SUBMITTER: Yang Z

PROVIDER: S-EPMC3702323 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of a thermostable GDSL-family esterase, EstL5, from Geobacillus thermodenitrificans T2.

Yang Zhenxing Z Zhang Yong Y Qiu Rui R Huang Jing J Ji Chaoneng C

Acta crystallographica. Section F, Structural biology and crystallization communications 20130628 Pt 7

The novel thermostable esterase EstL5 belonging to the GDSL family exhibits a unique cold-adaptation feature at low temperatures. To better understand its biochemical and enzymatic properties, recombinant EstL5 protein was purified and crystallized using the vapour-diffusion method. The EstL5 crystals diffracted X-rays to 2.79 Å resolution using a synchrotron-radiation source, belonged to the tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 101.51, c = 124.22 Å, and are ...[more]

PMID: 23832206

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