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

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14008371

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  1. Ministry of Education, Culture, Sports, Science and Technology, Japan,
  2. CREST, Japan Science and Technology Agency
  3. Grants-in-Aid for Scientific Research [23241068, 26560428] Funding Source: KAKEN

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AntE from Streptomyces sp. NRRL 2288 is a crotonyl-CoA carboxylase/reductase that catalyzes the reductive carboxylation of various alpha,beta-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 I2(1)2(1)2(1), with unit-cell parameters a = 76.4, b = 96.7, c = 129.6 angstrom, alpha = beta = gamma = 90.0 degrees. A diffraction data set was collected at the KEK Photon Factory to 2.29 angstrom resolution.

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