Cloning, overexpression, purification, crystallization and preliminary X‐ray diffraction analysis of glyceraldehyde‐3‐phosphate dehydrogenase from Antheraea mylitta

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|65|9|937-940

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.65, Iss.9, 2009-09, pp. : 937-940

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Abstract

Glyceraldehyde‐3‐phosphate dehydrogenase from Antheraea mylitta (AmGAPDH) was cloned in pQE30 vector, overexpressed in Escherichia coli M15 (pREP4) cells and purified to homogeneity. The protein was crystallized using the hanging‐drop vapour‐diffusion method. The crystals belonged to the orthorhombic space group I222, with unit‐cell parameters a = 85.81, b = 133.72, c = 220.37 Å. X‐ray diffraction data were collected and processed to a maximum resolution of 2.2 Å. The presence of three molecules in the asymmetric unit gave a Matthews coefficient (VM) of 2.80 Å3 Da−1, with a solvent content of 56.08%.

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