Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution
Abstract
The structure of the variable portions of a K-type Bence-Jones protein REI forming a dimer has been determined by X-ray diffraction to a resolution of 2.0 A. The structure has been refined using a constrained crystallographic refinement procedure. The final R value is 0.24 for 15000 significantly measured reflections; the estimated standard deviation of atomic positions is 0.09 A. A more objective assessment of the error in the atomic positions...
Paper Details
Title
Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution
Published Date
Nov 4, 1975
Journal
Volume
14
Issue
22
Pages
4943 - 4952
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