Crystallization and preliminary X-ray diffraction studies of glycine methyltransferase from rat liver.
Glycine methyltransferase from rat liver is a tetrameric enzyme with 292 amino acid residues in each identical subunit and catalyzes the AdoMet-dependent methylation of glycine to form sarcosine. The enzyme was crystallized by the hanging drop vapor diffusion method, using polyethylene glycol 4000 as a precipitant. The crystal belongs to the orthorhombic space group P2(1)2(1)2, with unit cell dimensions of a = 86.4, b = 175.7, c = 45.5 A and with two subunits in the asymmetric unit. The crystals diffract beyond 2.4 A resolution, and a set of 2.4 A resolution data were measured.
Fu
Z
Z
Department of Chemistry, University of Kansas, Lawrence 66045-0045, USA.
Takusagawa
F
F
Konishi
K
K
Takata
Y
Y
Fujioka
M
M
D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D050938:Glycine N-Methyltransferase; D008099:Liver / Q000201:enzymology*; D008780:Methyltransferases / Q000737:chemistry* / Q000378:metabolism; D051381:Rats; D012436:S-Adenosylmethionine / Q000378:metabolism
D012436:S-Adenosylmethionine; D008780:Methyltransferases; D050938:Glycine N-Methyltransferase