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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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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.
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container_issue 5
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container_title Acta crystallographica. Section D, Biological crystallography.
container_volume 54
creator 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.
description 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.
doi_str_mv 10.1107/S0907444998001887
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source Wiley-Blackwell Read & Publish Collection; Alma/SFX Local Collection
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
title Crystallization and preliminary X-ray analysis of Escherichia coli GlnK
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