Structure of a novel bence-jones protein (Rhe) fragment at 1·6 Å resolution
Abstract
The crystal structure of Rhe, a λ-type Bence-Jones protein fragment, has been solved and refined to a resolution of 1·6 Å. A model fragment consisting of the complete variable domain and the first three residues of the constant domain yields a crystallographic residual RF value of 0·149. The protein exists as a dimer both in solution and in the crystals. Although the “immunoglobulin fold” is generally preserved in the structure, there are...
Paper Details
Title
Structure of a novel bence-jones protein (Rhe) fragment at 1·6 Å resolution
Published Date
Jul 1, 1983
Journal
Volume
167
Issue
3
Pages
661 - 692
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