Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 62, Part 11 (November 2006)

crystallization communications

Acta Cryst. (2006). F62, 1097-1099 [ doi:10.1107/S1744309106037730 ]

Purification, crystallization and preliminary X-ray analysis of the glucosamine-6-phosphate N-acetyltransferase from human liver

J. Wang, Y.-F. Zhou, L.-F. Li, Y.-H. Liang and X.-D. Su

Abstract: Glucosamine-6-phosphate N-acetyltransferase from human liver, which catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amine of D-glucosamine 6-phosphate to form N-acetyl-D-glucosamine 6-phosphate, was expressed in a soluble form from Escherichia coli strain BL21 (DE3). The protein was purified to homogeneity using Ni²⁺-chelating chromatography followed by size-exclusion chromatography. Crystals of the protein were obtained by the hanging-drop vapour-diffusion method and diffracted to 2.6 Å resolution. The crystals belonged to space group P4₁2₁2 or P4₃2₁2, with unit-cell parameters a = b = 50.08, c = 142.88 Å.

Keywords: glucosamine-6-phosphate N-acetyltransferase.