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).
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| rdf:type | |
| rdfs:comment |
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).
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| skos:exactMatch | |
| uniprot:name |
Acta Crystallogr. D
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| uniprot:author |
Campbell S.A.,
Chackrewarthy S.,
Coggins J.R.,
Lapthorn A.J.,
Maclean J.,
Pollock K.
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| uniprot:date |
2000
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| uniprot:pages |
512-515
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| uniprot:title |
Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia coli.
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| uniprot:volume |
56
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| dc-term:identifier |
doi:10.1107/S0907444900002377
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