PMID:10739937
| Citation |
Maclean, J, Campbell, SA, Pollock, K, Chackrewarthy, S, Coggins, JR and Lapthorn, AJ (2000) Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:512-5 |
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| Abstract |
Shikimate dehydrogenase from Escherichia coli has been crystallized by the vapour-diffusion method using ammonium sulfate as a precipitant. Mass spectrometry confirmed the purity of the enzyme and dynamic light scattering was used to find the appropriate additives to yield a monodisperse enzyme solution. The crystals are monoclinic, space group C2, with unit-cell parameters a = 110.0, b = 139.8, c = 102.6 A, beta = 122.2 degrees (at 100 K). Native crystals diffract to 2.3 A in-house on a rotating-anode X-ray source. The asymmetric unit is likely to contain four molecules, related by 222 symmetry, corresponding to a packing density of 2.86 A(3) Da(-1). |
| Links | |
| Keywords |
Alcohol Oxidoreductases/chemistry; Alcohol Oxidoreductases/isolation & purification; Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Mass Spectrometry; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification |
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