Crystallization and preliminary X-ray analysis of Escherichia coli GlnK

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 Å and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1998-09, Vol.54 (5), p.996-998
Main Authors: Macpherson, Kirsty H. R., Xu, Yibin, Cheah, Eong, Carr, Paul D., Van Heeswijk, Wally C., Westerhoff, Hans V., Luque, Eva, Vasudevan, Subhash G., Ollis, David L.
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Carrier Proteins - chemistry
Carrier Proteins - isolation & purification
Crystallization
Crystallography, X-Ray
Escherichia coli - enzymology
Protein Conformation
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - isolation & purification
Signal Transduction
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Summary: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 Å and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63 with a = 57.45 Å and c = 54.79 Å. 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 Å.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444998001887