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  • Title: Crystallization and preliminary X-ray crystallographic studies of NADP-dependent 3-hydroxyisobutyrate dehydrogenase from Thermus thermophilus HB8.
    Author: Lokanath NK, Shiromizu I, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N.
    Journal: Acta Crystallogr D Biol Crystallogr; 2003 Dec; 59(Pt 12):2294-6. PubMed ID: 14646099.
    Abstract:
    3-Hydroxyisobutyrate, a central metabolite in the valine catabolic pathway, is reversibly oxidized to methylmalonate semialdehyde by a specific NADP-dependent dehydrogenase (HIBADH). HIBADH from Thermus thermophilus HB8 has been overexpressed in Escherichia coli and crystallized by the microbatch method using lithium chloride as a precipitant at 296 K. X-ray diffraction data have been collected to 1.80 A resolution at 100 K using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 85.878, b = 106.367, c = 168.639 A. A homotetramer of HIBADH is likely to be present in the asymmetric unit, giving a V(M) of 3.0 A(3) Da(-1) and a solvent content of 59.3%.
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