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Crystallization and preliminary x‐ray diffraction studies of a monoclonal antibody fab fragment against foot‐and‐mouth disease virus and of its complex with the main antigenic site peptide
Author(s) -
Verdaguer Nuria,
Mateu Mauricio G.,
Bravo Jerónimo,
Tormo José,
Giralt Ernest,
Andreu David,
Domingo Esteban,
Fita Ignacio
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340180212
Subject(s) - monoclinic crystal system , ammonium sulfate , crystallography , chemistry , crystallization , foot and mouth disease virus , monoclonal antibody , immunoglobulin fab fragments , antigen , antibody , crystal structure , virus , virology , biology , chromatography , organic chemistry , genetics , immunology , complementarity determining region
The Fab fragment of the neutralizing monoclonal antibody SD6 elicited against foot‐and‐mouth disease virus (FMDV) C‐SBcl and its complex with a peptide, corresponding to the major antigenic site of FMDV (VPl residues 136–150, YTASARGDLAHLTTT), have been crystallized using the hanging drop vapor diffusion techniques. For the isolated Fab, crystals diffracting to 2.5 Å resolution were obtained at room temperature using ammonium sulfate as precipitant. These crystals are monoclinic, space group C2, and unit cell parameters a = 109.53 Å, b = 89.12 Å, c = 64.04 Å, and β = 112.9° and contain one Fab molecule per asymmetric unit. Crystals from the complex diffract, at least, to 2.8 Å resolution and were obtained, at room temperature, using PEG as precipitant. These crystals are monoclinic, space group P2, and unit cell parameters a = 56.11 Å, b = 60.67 Å, c = 143.45 Å, and β = 95.4°, Density packing considerations indicate that there are two Fab molecules in the asymmetric unit. © 1994 John Wiley & Sons, Inc.