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 deficiency of the liver-specific peroxisomal enzyme alanine:glyoxylate aminotransferase (AGT). In this study, the crystallization and preliminary crystallographic analysis of C-terminal His-tagged human AGT expressed in Escherichia coli is reported. At least two crystal forms were obtained using similar conditions for three different polymorphic variants, namely AGT, AGT[P11L] and AGT[P11L, I340M]. Complete data have been collected for all three AGT variants. The crystals of AGT[P11L] belong to space group P4₁2₁2 (or its enantiomorph), with unit-cell parameters a = b = 90.81, c = 142.62 Å, and diffract to a resolution of 2.8 Å.