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

Fred J. Stevens, Florence A. Westholm, Nicolas Panagiotopoulos, Alan Solomon, Marianne Schiffer

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)179-183
Number of pages5
JournalJournal of Molecular Biology
Volume147
Issue number1
DOIs
StatePublished - Mar 25 1981
Externally publishedYes

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Bence Jones Protein
Molecular Weight
Ammonium Sulfate
Amino Acid Sequence
Light
Proteins

All Science Journal Classification (ASJC) codes

  • Virology

Cite this

Preliminary crystallographic data on the human λIII Bence Jones protein dimer Cle. / Stevens, Fred J.; Westholm, Florence A.; Panagiotopoulos, Nicolas; Solomon, Alan; Schiffer, Marianne.

In: Journal of Molecular Biology, Vol. 147, No. 1, 25.03.1981, p. 179-183.

Research output: Contribution to journalArticle

Stevens, Fred J. ; Westholm, Florence A. ; Panagiotopoulos, Nicolas ; Solomon, Alan ; Schiffer, Marianne. / Preliminary crystallographic data on the human λIII Bence Jones protein dimer Cle. In: Journal of Molecular Biology. 1981 ; Vol. 147, No. 1. pp. 179-183.
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