Orthorhombic crystal system

Biology

Chromatography

Crystal structure

Biochemistry

Stereochemistry

Immunology

Polymer

Bence Jones protein

Genetics

Organic chemistry

Sequence (biology)

Crystallography

Dimer

Chemistry

Monomer

Ammonium sulfate

Immunoglobulin light chain

Antibody

Journal of Molecular Biology

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 null null null a = 113.0 null null A null null null , b = 72.3 null null A null null null , null null and null null c = 48.9 null null A null null null null . The asymmetric unit consists of a dimer with a molecular weight of ~ 46,000.

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