Crystallization and preliminary X-ray diffraction studies of nucleoside diphosphate kinase from Dictyostelium discoideum

C Dumas; G Lebras; V Wallet; M L Lacombe; M Véron; J Janin

doi:10.1016/0022-2836(91)90537-g

Crystallization and preliminary X-ray diffraction studies of nucleoside diphosphate kinase from Dictyostelium discoideum

J Mol Biol. 1991 Jan 20;217(2):239-40. doi: 10.1016/0022-2836(91)90537-g.

Authors

C Dumas¹, G Lebras, V Wallet, M L Lacombe, M Véron, J Janin

Affiliation

¹ Laboratoire de Biologie Physicochimique, Université Paris-Sud, Orsay, France.

PMID: 1846924
DOI: 10.1016/0022-2836(91)90537-g

Abstract

Nucleoside diphosphate kinase from the slime mold Dictyostelium discoideum is highly homologous to gene products that are involved in development in Drosophila and in oncogenesis in human cells. The cloned protein expressed in Escherichia coli has been purified and crystallized in a hexagonal space group with a = b = 74.9 A, c = 211.4 A. The asymmetric unit contains either one or two 17,000 Mr subunits of the hexamer.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallography
Dictyostelium / enzymology*
Nucleoside-Diphosphate Kinase / ultrastructure*
Protein Conformation
Recombinant Proteins / ultrastructure
X-Ray Diffraction

Substances

Recombinant Proteins
Nucleoside-Diphosphate Kinase