CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF PHOSPHO-ADENYLYLSULFATE (PAPS) REDUCTASE FROM ESCHERICHIA-COLI

Authors
MONTOYA G SVENSSON C SAVAGE H SCHWENN JD SINNING I
Citation
G. Montoya et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF PHOSPHO-ADENYLYLSULFATE (PAPS) REDUCTASE FROM ESCHERICHIA-COLI, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 281-283
Citations number
13
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
2
Pages
281 - 283
Database
ISI
SICI code
0907-4449(1998)54:<281:CAPDSO>2.0.ZU;2-1
Abstract
PAPS reductase from E. coli is involved in sulfur metabolism and catal yses the reduction of phospho-adenylyl-sulfate (PAPS) to sulfite. The protein has been cloned, overexpressed and purified from E. coli. Crys tallization experiments resulted in crystals suitable for X-ray diffra ction. The crystals belong to the orthorhombic space group C222(1) wit h cell dimensions a = 81.9, b = 97.4, c = 109.5 Angstrom, and contain one molecule per asymmetric unit. At cryogenic (100 K) temperatures th e crystals diffract to a resolution limit of 2.7 K using a rotating an ode and to 2.0 Angstrom at a synchrotron source.