Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 62, Part 12 (December 2006)

crystallization communications

Acta Cryst. (2006). F62, 1206-1208 [ doi:10.1107/S1744309106044186 ]

Purification, crystallization and preliminary X-ray diffraction studies of UDP-N-acetylglucosamine pyrophosphorylase from Candida albicans

D. Maruyama, Y. Nishitani, T. Nonaka, A. Kita, T. A. Fukami, T. Mio, H. Yamada-Okabe, T. Yamada-Okabe and K. Miki

Abstract: UDP-N-acetylglucosamine pyrophosphorylase (UAP) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine. UAP from Candida albicans was purified and crystallized by the sitting-drop vapour-diffusion method. The crystals of the substrate and product complexes both diffract X-rays to beyond 2.3 Å resolution using synchrotron radiation. The crystals of the substrate complex belong to the triclinic space group P1, with unit-cell parameters a = 47.77, b = 62.89, c = 90.60 Å, [alpha] = 90.01, [beta] = 97.72, [gamma] = 92.88°, whereas those of the product complex belong to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 61.95, b = 90.87, c = 94.88 Å.

Keywords: UDP-N-acetylglucosamine pyrophosphorylase; Candida albicans.