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Crystallization and preliminary x-ray diffraction studies of guanidinoacetate methyltransferase from rat liver
1Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045-0045, USA.
Acta Crystallographica. Section D, Biological Crystallography
|October 26, 1999
Abstract:
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 P2(1), with unit-cell parameters a = 54.8, b = 162.5, c = 56.1 A, beta = 96.8 (1) degrees at 93 K, and typically diffract beyond 2.8 A.