Crystal and molecular structure of the dimer of variable domains of the Bence-Jones protein ROY
Abstract
The crystal and molecular structure of the dimer of variable domains of the Bence-Jones protein ROY has been determined by Patterson function search procedures, using the known structure of the protein REI. The structure has been partially refined at 3.0 A resolution to a crystallographic null R -factor value of 0.33. One of the 18 residues differentiating ROY from REI is the substitution of Tyr96 for Leu96, a substitution which makes the...
Paper Details
Title
Crystal and molecular structure of the dimer of variable domains of the Bence-Jones protein ROY
Published Date
Oct 1, 1977
Journal
Volume
116
Issue
1
Pages
73 - 79
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