Crystallization and preliminary X‐ray diffraction analysis of AntE, a crotonyl‐CoA carboxylase/reductase from Streptomyces sp. NRRL 2288. Issue 6 (1st June 2014)

• Record Type: Journal Article
• Authors: Zhang, Lihan; Chen, Jing; Mori, Takahiro; Yan, Yan; Liu, Wen; Abe, Ikuro
• Is Part Of: Acta crystallographica. Volume 70:Issue 6(2014:Jun.)
• Page Start: 734
• Page End: 737
• Publication Date: 2014-06-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14008371
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>AntE from <italic>Streptomyces</italic> 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 <italic>Escherichia coli</italic> was crystallized by the sitting‐drop vapour‐diffusion method. The crystals belonged to space group <italic>I</italic>222 or <italic>I</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 76.4, <italic>b</italic> = 96.7, <italic>c</italic> = 129.6 Å, α = β = γ = 90.0°. A diffraction data set was collected at the KEK Photon Factory to 2.29 Å resolution.</p> </abstract>