Crystallographic refinement of the three-dimensional structure of the FabD1. 3-lysozyme complex at 2.5-A resolution
TO Fischmann, GA Bentley, TN Bhat, G Boulot… - Journal of Biological …, 1991 - ASBMB
The three-dimensional crystal structure of the complex between the Fab from the
monoclonal anti-lysozyme antibody D1. 3 and the antigen, hen egg white lysozyme, has
been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution.
The antibody contacts the antigen with residues from all its complementarity determining
regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant
making hydrogen bonds and van der Waals interactions with the antibody. Water molecules …
monoclonal anti-lysozyme antibody D1. 3 and the antigen, hen egg white lysozyme, has
been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution.
The antibody contacts the antigen with residues from all its complementarity determining
regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant
making hydrogen bonds and van der Waals interactions with the antibody. Water molecules …
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