ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Dehydroepiandrosterone sulfotransferase converts dehydroepiandrosterone (DHEA) and some other steroids to their sulfonated forms. The human enzyme has been crystallized in the presence of substrate (DHEA) alone, in the presence of substrate and non-sulfated cofactor analogue (PAP) and in the absence of both substrate and PAP in our laboratory, with data sets collected at a synchrotron source. The crystals of the uncomplexed form belong to the orthorhombic space group C2221, with unit-cell parameters a = 85.26, b = 87.69, c = 108.20 Å and data 99.2% complete to 2.35 Å resolution. The DHEA complex crystallizes in the orthorhombic space group P21212, with unit-cell parameters a = 74.46, b = 127.49, c = 44.59 Å and data 92.9% complete to 2.15 Å resolution. The ternary complex crystallizes in the orthorhombic space group P212121, with unit-cell parameters a = 62.25, b = 87.28, c = 138.86 Å and data 98.6% complete to 2.50 Å resolution. Preliminary molecular-replacement solutions indicate significant variations in dimer formation.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444901010964
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