Purification, crystallization and preliminary crystallographic characterization of the α2,6‐sialyltransferase from Photobacterium sp. JT‐ISH‐224
Sialyltransferases transfer sialic acid from cytidine‐5‐monophospho‐N‐acetylneuraminic acid (CMP‐NeuAc) to the nonreducing termini of the oligosaccharyl structures of various glycoproteins and glycolipids. The newly cloned α2,6‐sialyltransferase from Photobacterium sp. JT‐ISH‐224 (from the Vibrionaceae family) is composed of two domains: an unknown N‐terminal domain and a catalytic C‐terminal domain which shares significant homology with the Pasteurella multocida multifunctional sialyltransferase. The putative mature form of JT‐ISH‐224 α2,6‐sialyltransferase was overproduced in Escherichia coli, purified and crystallized using the hanging‐drop vapour‐diffusion method at 293 K. The crystal belonged to space group P3121 or P3221, with unit‐cell parameters a = b = 90.29, c = 204.33 Å. X‐ray diffraction data were collected to 2.5 Å resolution.
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