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Crystallization and preliminary X-ray analysis of Escherichia coli GlnK
K H MacPherson1, Y Xu, E Cheah
1Research School of Chemistry, Australian National University, Canberra ACT 0200, Australia.
Acta Crystallographica. Section D, Biological Crystallography
|October 3, 1998
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.