Crystallization and preliminary X-ray analysis of Escherichia coli GlnK
Acta Crystallographica Section D
Volume 54, Issue 5, pages 996–998, September 1998
How to Cite
Macpherson, K. H. R., Xu, Y., Cheah, E., Carr, P. D., Van Heeswijk, W. C., Westerhoff, H. V., Luque, E., Vasudevan, S. G. and Ollis, D. L. (1998), Crystallization and preliminary X-ray analysis of Escherichia coli GlnK. Acta Crystallographica Section D, 54: 996–998. doi: 10.1107/S0907444998001887
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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.