Abstract
Acetohydroxy acid isomeroreductase (EC 1.1.1.86) is one of the enzymes involved in branched-chain amino acid biosynthesis. The enzyme from spinach (Spinacia oleracea) leaves has been crystallized using the hanging drop vapour diffusion method. The free enzyme crystallized from polyethylene glycol solutions, but these crystals were unsuitable for X-ray diffraction analysis. In the presence of NADPH, Mg2+ and a reaction intermediate analogue (2-dimethylphosphinoyl-2-hydroxy acetic acid (Hoe 704) or N -hydroxy-N-isopropyloxamate (IpOHA)), much better crystals were obtained. Crystals grown from ammonium sulphate belong to space group P 21 with cell dimensions a = 193·78(7) Å,b = 63·69(2) Å,c = 112·84(1) Å and β = 121·22(1)°. The molecular that the protein, the volume of the unit cell, and crystal density measurements indicated that the asymmetric unit contains two dimers. X-ray diffraction patterns showed measurable reflections to beyond 2·5 Å.
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