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 P4(1)2(1)2 (or its enantiomorph), with unit-cell parameters a = b = 90.81, c = 142.62 A, and diffract to a resolution of 2.8 A.
Zhang
X
X
Department of Biology, University College London, Gower Street, London WC1E 6BT, England.
Roe
S M
SM
Pearl
L H
LH
Danpure
C J
CJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D000637:Transaminases / Q000737:chemistry* / Q000235:genetics
D011994:Recombinant Proteins; D000637:Transaminases; C019635:Alanine-glyoxylate transaminase