TRIGONAL CRYSTALS OF PORCINE MITOCHONDRIAL ASPARTATE-AMINOTRANSFERASE

Crystals suitable for X-ray analysis of procine mitochondrial aspartate aminotransferase in the closed conformation were obtained after the apoenzyme was reconstituted with N-5′-phosphopyridoxyl-l-aspartate, an inhibitor in which the cofactor is covalently bound to the substrate. This results in a crystal form that has not been encountered previously in studies of aspartate aminotransferases. The crystals belong to the trigonal space group P3121 (or the enantiomeric P3221) with unit cell dimensions a=b=202·0 , c=58·0 , α=β=900, ψ=1200 and contain one dimer in the asymmetric unit. © 1990, Academic Press Limited. All rights reserved.