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Crystallization and preliminary X-ray diffraction studies of guanidinoacetate methyltransferase from rat liver
Komoto, Junichi Huang, Yafei Hu, Yongbo Takata, Yoshimi Konishi, Kiyoshi Ogawa, Hirofumi Gomi, Tomoharu Fujioka, Motoji Takusagawa, Fusao
Komoto, Junichi
Huang, Yafei
Hu, Yongbo
Takata, Yoshimi
Konishi, Kiyoshi
Ogawa, Hirofumi
Gomi, Tomoharu
Fujioka, Motoji
Takusagawa, Fusao
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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 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.
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1999-01-01
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International Union of Crystallography
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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.