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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 Å resolution at 100 K using synchrotron radiation. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 85.878, b = 106.367, c = 168.639 Å. A homotetramer of HIBADH is likely to be present in the asymmetric unit, giving a VM of 3.0 Å3 Da-1 and a solvent content of 59.3%.

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