Crystallization and preliminary X-ray crystallographic analysis of the alpha-2,6-sialyltransferase PM0188 from Pasteurella multosida

Abstract

Sialyltransferase is an enzyme that transfers the sialic acid moiety from cytidine-5-monophospho-N-acetylneuraminic acid (CMP-NeuAc) to the carbohydrate group of various glycoproteins. These glycoproteins are involved in inflammation, embryogenesis, immune defence and metastasis of cancer cells by cell-cell interactions or cell-matrix interactions. The alpha-2,6-sialyltransferase PM0188 from Pasteurella multocida was purified using affinity-column chromatographic methods and crystallized using the hanging-drop vapour-diffusion method at 293 K. MAD data were collected to 1.9 A resolution from an SeMet-substituted crystal. The crystal belongs to space group P2(1), with unit-cell parameters a = 52.9, b = 61.0, c = 64.6 A, alpha = gamma = 90, beta = 112.3 degrees. Assuming the presence of one molecule in the asymmetric unit, the solvent content is estimated to be about 45%.