Characterization and preliminary crystallographic data on the VL-related fragment of the human κI Bence Jones protein Wat

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

Research output: Contribution to journalArticle

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Abstract

A "naturally occurring" human κI VL dimer, designated Wat, has been isolated and crystallized. Protein Wat consists of two non-covalently bound monomers, each having a molecular weight of ~ 11,500. The monomer subunit is composed of an entire variable region light chain (VL) domain closely homologous to that of the κI Bence Jones protein Roy (Hilschmann & Craig, 1965) as evidenced from amino acid composition, tryptic peptide map, and sequence analysis. Immunochemical studies substantiated that protein Wat is of the κ chain subgroup κI and lacks the isotypic and allotypic antigenic determinants associated with the κ constant region light chain domain. Two types of crystals of VL dimer Wat were obtained from ammonium sulfate or polyethylene glycol solutions. The type I crystals have unit cell dimensions of a = b = 82.6 A ̊, c = 60.3 A ̊, and the space group is hexagonal P62 or P64. The asymmetric unit consists of one VL dimer; the fractional volume of unit cell occupied by solvent is 0.51. The unit cell dimensions of the type II crystals are a = b = 1,08.3 A ̊, c = 108.8 A ̊; the space group is hexagonal P6122 or P6522. Three variable domains constitute the asymmetric unit of the type II crystals; the fractional value of the solvent (0.52) is compatible with the value obtained for the type I crystals.

Original languageEnglish (US)
Pages (from-to)185-193
Number of pages9
JournalJournal of Molecular Biology
Volume147
Issue number1
DOIs
StatePublished - Mar 25 1981
Externally publishedYes

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Bence Jones Protein
Light
Protein Sequence Analysis
Ammonium Sulfate
Cell Size
Epitopes
Proteins
Molecular Weight
Amino Acids

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

Characterization and preliminary crystallographic data on the VL-related fragment of the human κI Bence Jones protein Wat. / Stevens, Fred J.; Westholm, Florence A.; Panagiotopoulos, Nicolas; Schiffer, Marianne; Popp, Raymond A.; Solomon, Alan.

In: Journal of Molecular Biology, Vol. 147, No. 1, 25.03.1981, p. 185-193.

Research output: Contribution to journalArticle

Stevens, Fred J. ; Westholm, Florence A. ; Panagiotopoulos, Nicolas ; Schiffer, Marianne ; Popp, Raymond A. ; Solomon, Alan. / Characterization and preliminary crystallographic data on the VL-related fragment of the human κI Bence Jones protein Wat. In: Journal of Molecular Biology. 1981 ; Vol. 147, No. 1. pp. 185-193.
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abstract = "A {"}naturally occurring{"} human κI VL dimer, designated Wat, has been isolated and crystallized. Protein Wat consists of two non-covalently bound monomers, each having a molecular weight of ~ 11,500. The monomer subunit is composed of an entire variable region light chain (VL) domain closely homologous to that of the κI Bence Jones protein Roy (Hilschmann & Craig, 1965) as evidenced from amino acid composition, tryptic peptide map, and sequence analysis. Immunochemical studies substantiated that protein Wat is of the κ chain subgroup κI and lacks the isotypic and allotypic antigenic determinants associated with the κ constant region light chain domain. Two types of crystals of VL dimer Wat were obtained from ammonium sulfate or polyethylene glycol solutions. The type I crystals have unit cell dimensions of a = b = 82.6 A ̊, c = 60.3 A ̊, and the space group is hexagonal P62 or P64. The asymmetric unit consists of one VL dimer; the fractional volume of unit cell occupied by solvent is 0.51. The unit cell dimensions of the type II crystals are a = b = 1,08.3 A ̊, c = 108.8 A ̊; the space group is hexagonal P6122 or P6522. Three variable domains constitute the asymmetric unit of the type II crystals; the fractional value of the solvent (0.52) is compatible with the value obtained for the type I crystals.",
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