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

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 α‐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 Å resolution from an SeMet‐substituted crystal. The crystal belongs to space group P 2 1 , with unit‐cell parameters a  = 52.9, b = 61.0, c = 64.6 Å, α = γ = 90, β = 112.3°. Assuming the presence of one molecule in the asymmetric unit, the solvent content is estimated to be about 45%.