Crystallization and preliminary X-ray diffraction analysis of AntE, a crotonyl-CoA carboxylase/reductase from Streptomyces sp. NRRL 2288

AntE from Streptomyces sp. NRRL 2288 is a crotonyl-CoA carboxylase/reductase that catalyzes the reductive carboxylation of various α,β-unsaturated acyl-CoAs to provide the building block at the C7 position for antimycin A biosynthesis. Recombinant AntE expressed in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group I222 or I212121, with unit-cell parameters a = 76.4, b = 96.7, c = 129.6 Å, α = β = γ = 90.0°. A diffraction data set was collected at the KEK Photon Factory to 2.29 Å resolution.

Source: Acta Crystallographica Section F - May 10, 2014 Category: Biochemistry Authors: Zhang, L.Chen, J.Mori, T.Yan, Y.Liu, W.Abe, I. Tags: AntE crotonyl-CoA carboxylase/reductase polyketide Streptomyces sp. NRRL 2288 crystallization communications Source Type: research