CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF ESCHERICHIA-COLI GLNK

Authors
MACPHERSON KHR XU YB CHEAH E CARR PD VANHEESWIJK WC WESTERHOFF HV LUQUE E VASUDEVAN SG OLLIS DL
Citation
Khr. Macpherson et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF ESCHERICHIA-COLI GLNK, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 996-998
Citations number
16
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
5
Pages
996 - 998
Database
ISI
SICI code
0907-4449(1998)54:<996:CAPAOE>2.0.ZU;2-T
Abstract
The trimeric sinal-transduction protein GlnK, from Escherichia coli, h as been over-expressed, purified to homogeneity and crystallized. The crystals belong to space group P2(1)3 with a = 85.53 Angstrom and have two subunits in the asymmetric unit. The complex of GlnK with ATP cry stallized in space group P6(3) with a = 57.45 Angstrom and c = 54.79 A ngstrom. These crystals have a single subunit in the asymmetric unit. High-quality diffraction data from crystals of GlnK and the Glnk compl ex have been collected to 2.0 Angstrom.