Preliminary Crystallographic Data on the Human λIII Bence Jones Protein Dimer Cle
Document Type
Article
Publication Date
3-25-1981
Description
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 Å 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.
Citation Information
Stevens, Fred J.; Westholm, Florence A.; Panagiotopoulos, Nicolas; Solomon, Alan; and Schiffer, Marianne. 1981. Preliminary Crystallographic Data on the Human λIII Bence Jones Protein Dimer Cle. Journal of Molecular Biology. Vol.147(1). 179-183. https://doi.org/10.1016/0022-2836(81)90085-1 PMID: 6790716 ISSN: 0022-2836