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Acetohydroxy acid isomeroreductase (AHIR) is involved in the biosynthetic pathway of branched-chain amino acids in microorganisms and plants. AHIR from Pseudomonas aeruginosa has been overexpressed in Escherichia coli and crystallized at 297 K using potassium/sodium tartrate as a precipitant. X-ray diffraction data have been collected to 2.0 Å resolution at 100 K using synchrotron radiation. The crystals belong to the cubic space group P213, with unit-cell parameters a = b = c = 184.38 Å, α = β = γ = 90°. Six monomers are present in the asymmetric unit, giving a VM of 2.34 Å3 Da−1 and a solvent content of 47.4%.

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