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. 1998 Sep 1;54(Pt 5):996-8.
doi: 10.1107/s0907444998001887.

Crystallization and preliminary X-ray analysis of Escherichia coli GlnK

K H MacPherson  1 , Y Xu, E Cheah, P D Carr, W C van Heeswijk, H V Westerhoff, E Luque, S G Vasudevan, D L Ollis
Affiliations

Crystallization and preliminary X-ray analysis of Escherichia coli GlnK

K H MacPherson et al. Acta Crystallogr D Biol Crystallogr. .

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.

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