Crystallization and preliminary crystallographic analysis of human alanine: glyoxylate aminotransferase and its polymorphic variants

The human hereditary disease primary hyperoxaluria type 1 is caused by a de ficiency of the liver-specific peroxisomal enzyme alanine: glyoxylate amino transferase (AGT). In this study, the crystallization and preliminary cryst allographic analysis of C-terminal His-tagged human AGT expressed in Escher ichia coli is reported. At least two crystal forms were obtained using simi lar conditions for three different polymorphic variants, namely AGT, AGT[P1 1L] and AGT[P11L, I340M]. Complete data have been collected for all three A GT variants. The crystals of AGT[P11L] belong to space group P4(1)2(1)2 (or its enantiomorph), with unit-cell parameters a=b=90.81, c=142.62 Angstrom, and diffract to a resolution of 2.8 Angstrom.