Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver

Komoto, JunichiHuang, YafeiHu, YongboTakata, YoshimiKonishi, KiyoshiOgawa, HirofumiGomi, TomoharuFujioka, MotojiTakusagawa, Fusao2015-03-232015-03-231999-01-01Komoto, Junichi et al. (1999). "Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver." Acta Crystallographica D, 55(11):1928-1929. http://www.dx.doi.org/10.1107/S0907444999010318.0365-110Xhttps://hdl.handle.net/1808/17175This is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S0907444999010318.Guanidinoacetate methyltransferase is the enzyme which catalyzes the last step of creatine biosynthesis. The enzyme is found ubiquitously and in abundance in the livers of all vertebrates. Recombinant rat-liver guanidinoacetate methyltransferase has been crystallized with guanidinoacetate and S-adenosylhomocysteine. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 Å, [beta] = 96.8 (1)° at 93 K, and typically diffract beyond 2.8 Å.Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liverArticle10.1107/S0907444999010318openAccess