Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver
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Issue Date
1999-01-01Article Version
Scholarly/refereed, publisher version
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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.
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This is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S0907444999010318.
ISSN
0365-110XCollections
Citation
Komoto, 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.
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