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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 57; no. 12; pp. 1936 - 1937
• Main Authors: Zhang, Xiaoxuan, Roe, S. Mark, Pearl, Laurence H., Danpure, Christopher J.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-12-2001
• Subjects: alanine:glyoxylate aminotransferase; Crystallization; Crystallography, X-Ray; Humans; Polymorphism, Genetic; primary hyperoxaluria type 1; Protein Conformation; Recombinant Proteins - chemistry; Transaminases - chemistry; Transaminases - genetics
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444901017334

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.