Crystallographic data on a complete κ-type human Bence-Jones protein

Marianne Schiffer, Florence A. Westholm, Nicolas Panagiotopoulos, Alan Solomon

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

A complete human κ-type Bence-Jones protein (Fin) has been isolated and crystallized. Immunochemical and physicochemical characterization of protein Fin indicates that it is of the κ-chain subgroup, κII, and that it consists of two non-covalently bound intact monomers having a molecular weight of ~23,000 Crystals of Bence-Jones protein Fin obtained from ammonium sulfate solutions have the orthorhombic space group P212121 with cell dimensions a = 132.0 A ̊, b = 93.3 A ̊, and c = 42.3 A ̊. The asymmetric unit consists of a dimer of molecular weight ~46,000.

Original languageEnglish (US)
Pages (from-to)287-290
Number of pages4
JournalJournal of Molecular Biology
Volume124
Issue number1
DOIs
StatePublished - Sep 5 1978
Externally publishedYes

Fingerprint

Bence Jones Protein
Molecular Weight
Ammonium Sulfate
Proteins

All Science Journal Classification (ASJC) codes

  • Virology

Cite this

Crystallographic data on a complete κ-type human Bence-Jones protein. / Schiffer, Marianne; Westholm, Florence A.; Panagiotopoulos, Nicolas; Solomon, Alan.

In: Journal of Molecular Biology, Vol. 124, No. 1, 05.09.1978, p. 287-290.

Research output: Contribution to journalArticle

Schiffer, Marianne ; Westholm, Florence A. ; Panagiotopoulos, Nicolas ; Solomon, Alan. / Crystallographic data on a complete κ-type human Bence-Jones protein. In: Journal of Molecular Biology. 1978 ; Vol. 124, No. 1. pp. 287-290.
@article{3b0a20b9970d410b83ab26557ee39890,
title = "Crystallographic data on a complete κ-type human Bence-Jones protein",
abstract = "A complete human κ-type Bence-Jones protein (Fin) has been isolated and crystallized. Immunochemical and physicochemical characterization of protein Fin indicates that it is of the κ-chain subgroup, κII, and that it consists of two non-covalently bound intact monomers having a molecular weight of ~23,000 Crystals of Bence-Jones protein Fin obtained from ammonium sulfate solutions have the orthorhombic space group P212121 with cell dimensions a = 132.0 A ̊, b = 93.3 A ̊, and c = 42.3 A ̊. The asymmetric unit consists of a dimer of molecular weight ~46,000.",
author = "Marianne Schiffer and Westholm, {Florence A.} and Nicolas Panagiotopoulos and Alan Solomon",
year = "1978",
month = "9",
day = "5",
doi = "10.1016/0022-2836(78)90161-4",
language = "English (US)",
volume = "124",
pages = "287--290",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Crystallographic data on a complete κ-type human Bence-Jones protein

AU - Schiffer, Marianne

AU - Westholm, Florence A.

AU - Panagiotopoulos, Nicolas

AU - Solomon, Alan

PY - 1978/9/5

Y1 - 1978/9/5

N2 - A complete human κ-type Bence-Jones protein (Fin) has been isolated and crystallized. Immunochemical and physicochemical characterization of protein Fin indicates that it is of the κ-chain subgroup, κII, and that it consists of two non-covalently bound intact monomers having a molecular weight of ~23,000 Crystals of Bence-Jones protein Fin obtained from ammonium sulfate solutions have the orthorhombic space group P212121 with cell dimensions a = 132.0 A ̊, b = 93.3 A ̊, and c = 42.3 A ̊. The asymmetric unit consists of a dimer of molecular weight ~46,000.

AB - A complete human κ-type Bence-Jones protein (Fin) has been isolated and crystallized. Immunochemical and physicochemical characterization of protein Fin indicates that it is of the κ-chain subgroup, κII, and that it consists of two non-covalently bound intact monomers having a molecular weight of ~23,000 Crystals of Bence-Jones protein Fin obtained from ammonium sulfate solutions have the orthorhombic space group P212121 with cell dimensions a = 132.0 A ̊, b = 93.3 A ̊, and c = 42.3 A ̊. The asymmetric unit consists of a dimer of molecular weight ~46,000.

UR - http://www.scopus.com/inward/record.url?scp=0018261302&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018261302&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(78)90161-4

DO - 10.1016/0022-2836(78)90161-4

M3 - Article

VL - 124

SP - 287

EP - 290

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -