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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Crystallization and preliminary X-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase.

Dihydrodiol dehydrogenase catalyzes the NADP(+)-linked oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols and exists in multiple forms in mammalian tissues. The dimeric form of mammalian dihydrodiol dehydrogenase has a primary structure distinct from the previously known mammalian enzymes and may constitute a novel protein family with the prokaryotic proteins. Monkey kidney dimeric dihydrodiol dehydrogenase was crystallized from buffered ammonium phosphate solution using the hanging-drop vapour-diffusion method. The crystals diffract to 2.65 A resolution in the laboratory and belong to the hexagonal P6(1)22 or P6(5)22 space group, with unit-cell parameters a = b = 122.8, c = 121.3 A, alpha = beta = 90, gamma = 120 degrees.[1]

References

  1. Crystallization and preliminary X-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase. El-Kabbani, O., Chung, R.P., Ramsland, P.A., Asada, Y., Ishikura, S., Usami, N., Hara, A. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
 
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