Preliminary crystallographic data on the human λIII Bence Jones protein dimer Cle

Published on Mar 1, 1981in Journal of Molecular Biology5.067
· DOI :10.1016/0022-2836(81)90085-1
Fred J. Stevens31
Estimated H-index: 31
(Argonne National Laboratory),
Florence A. Westholm7
Estimated H-index: 7
(Argonne National Laboratory)
+ 2 AuthorsMarianne Schiffer40
Estimated H-index: 40
(Argonne National Laboratory)
A complete human λ Bence Jones protein dimer (Cle) has been isolated and crystallized. Protein Cle was characterized immunochemically and chemically as having a variable region amino acid sequence associated with light chains of the λ chain subgroup, λIII, and a constant region sequence characteristic of “non-Mcg” type λ chains. Bence Jones protein Cle contains two covalently bound intact monomers, each having a molecular weight of ~23,000. Crystals of Bence Jones protein Cle, obtained from ammonium sulfate solutions, diffract to 2.6 A resolution and have the orthorhombic space group P212121 with cell dimensions a = 113.0 A, b = 72.3 A, and c = 48.9 A. The asymmetric unit consists of a dimer with a molecular weight of ~ 46,000.
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