Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase
Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. E...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1996-11, Vol.52 (6), p.1188-1190 |
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container_title | Acta crystallographica. Section D, Biological crystallography. |
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creator | Cowan-Jacob, S. W. Rahuel, J. Nagai, A. Iwasaki, G. Ohta, D. |
description | Recombinant Brassica oleracea histidinol dehydrogenase (HDH) has been crystallized in various space groups using the method of vapour diffusion. The presence or absence of inhibitors and substrates as well as the use of different precipitants has enabled the growth of five different crystal forms. Extensive searches with the first crystal form (A) failed to produce any useful heavy‐atom derivatives, mainly because of the instability of the crystals. This provoked the search for further crystal forms in the hope of finding more suitable crystals. At least two of these crystal forms are of interest for further study. |
doi_str_mv | 10.1107/S0907444996008396 |
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title | Crystallization and preliminary crystallographic analysis of cabbage histidinol dehydrogenase |
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