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Protein Science, Vol 6, Issue 3 717-721, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Expression, crystallization, and preliminary X-ray analysis of a sialic acid-binding fragment of sialoadhesin in the presence and absence of ligand

A. P. MAY, R. C. ROBINSON, R. T. APLIN, P. BRADFIELD, P. R. CROCKER and E. Y. JONES
Laboratory of Molecular Biophysics, University of Oxford, Oxford, United Kingdom Oxford Centre for Molecular Sciences, University of Oxford, Oxford, United Kingdom

Sialoadhesin is a macrophage-restricted cell surface receptor, consisting of 17 immunoglobulin domains, which mediates cell adhesion via the recognition of specific sialylated glycoconjugates. A functional fragment of sialoadhesin, comprising the N-terminal immunoglobulin domain, has been expressed in Chinese hamster ovary cells as both native (SnD1) and selenomethionyl (Se-SnD1) stop protein. The successful production of 86% selenomethionine-incorporated protein represents a rare example of production of selenium-labeled protein in mammalian cells. SnD1 and Se-SnD1 have been crystallized in the absence of ligand, and SnD1 has also been crystallized in the presence of its ligand 2,3 sialyllactose. The ligand-free crystals of SnD1 and Se-SnD1 were isomorphous, of space group P3(1)21 or P3(2)21, with unit cell dimensions a = b = 38.9 A, c = 152.6 A, {alpha} = {beta} = 90{deg}, {gamma} = 120{deg}, and diffracted to a maximum resolution of 2.6 A. Cocrystals containing 2,3 sialyllactose diffracted to 1.85 A at a synchrotron source and belong to space group P2(1)2(1)2(1), with unit cell dimensions a = 40.9 A, b = 97.6 A, c = 101.6 A, {alpha} = {beta} = {gamma} = 90{deg}.
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