Abstract
In the NAD biosynthetic pathway, nicotinamide phosphoribosyltransferase (NMPRTase; EC 2.4.2.12) plays an important role in catalyzing the synthesis of nicotinamide mononucleotide from nicotinamide and 5′-phosphoribosyl- 1′-pyrophosphate. Because the diffraction pattern of the initally obtained crystals was not suitable for structure analysis, the crystal quality was improved by successive use of the microseeding technique. The resultant crystals diffracted to 2.0 Å resolution. These crystals belonged to space group P21, with unit-cell parameters a = 60.56, b = 106.40, c = 82.78 Å. Here, the crystallization of human NMPRTase is reported in the free form; the crystals should be useful for inhibitor-soaking experiments on the enzyme. © International Union of Crystallography 2007.
Author supplied keywords
Cite
CITATION STYLE
Takahashi, R., Nakamura, S., Yoshida, T., Kobayashi, Y., & Ohkubo, T. (2007). Crystallization of human nicotinamide phosphoribosyltransferase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(5), 375–377. https://doi.org/10.1107/S1744309107006069
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.