Crystallization and preliminary X-ray analysis of Escherichia coli GlnK.

Acta crystallographica. Section D, Biological crystallography ·Vol. 54 ·No. Pt 5 ·1998-09-01 ·Pages 996-8

MacPherson KH, Xu Y, Cheah E, Carr PD, van Heeswijk WC, Westerhoff HV, Luque E, Vasudevan SG, Ollis DL

Abstract

The trimeric signal-transduction protein GlnK, from Escherichia coli, has been over-expressed, purified to homogeneity and crystallized. The crystals belong to space group P213 with a = 85.53 A and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63 with a = 57.45 and c = 54.79 A. These crystals have a single subunit in the asymmetric unit. High-quality diffraction data from crystals of GlnK and the GlnK complex have been collected to 2.0 A.

MeSH Terms

Bacterial Proteins/chemistry,isolation & purification Carrier Proteins/chemistry,isolation & purification Crystallization Crystallography, X-Ray Escherichia coli/enzymology Protein Conformation Recombinant Fusion Proteins/chemistry,isolation & purification Signal Transduction

Chemicals

Bacterial Proteins Carrier Proteins GlnK protein, Azorhizobium caulinodans Recombinant Fusion Proteins

Authors & Affiliations

9 authors, click to expand affiliations / ORCID

MacPherson K H

Research School of Chemistry, Australian National University, Canberra ACT 0200, Australia.

Xu Y

Cheah E

Carr P D

van Heeswijk W C

Westerhoff H V

Luque E

Vasudevan S G

Ollis D L

Article Info

Journal

Acta crystallographica. Section D, Biological crystallography

Abbr.

Acta Crystallogr D Biol Crystallogr

ISSN

0907-4449

DOI

10.1107/s0907444998001887

Published

1998-09-01

Pages

996-8

Language

English

Region

United States

NLM ID

9305878

Subset

External Links

PubMed source DOI: 10.1107/s0907444998001887 View journal details

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Crystallization and preliminary X-ray analysis of Escherichia coli GlnK.

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