Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli

G Montoya; C Svensson; H Savage; J D Schwenn; I Sinning

doi:10.1107/s0907444997010019

Crystallization and preliminary X-ray diffraction studies of phospho-adenylylsulfate (PAPS) reductase from E. coli

Acta Crystallogr D Biol Crystallogr. 1998 Mar 1;54(Pt 2):281-3. doi: 10.1107/s0907444997010019.

Authors

G Montoya¹, C Svensson, H Savage, J D Schwenn, I Sinning

Affiliation

¹ European Molecular Biology Laboratory, Structural Biology Programme, 69117 Heidelberg, Germany.

PMID: 9761895
DOI: 10.1107/s0907444997010019

Abstract

PAPS reductase from E. coli is involved in sulfur metabolism and catalyses the reduction of phospho-adenylyl-sulfate (PAPS) to sulfite. The protein has been cloned, overexpressed and purified from E. coli. Crystallization experiments resulted in crystals suitable for X-ray diffraction. The crystals belong to the orthorhombic space group C2221 with cell dimensions a = 81.9, b = 97.4, c = 109.5 A, and contain one molecule per asymmetric unit. At cryogenic (100 K) temperatures the crystals diffract to a resolution limit of 2.7 A using a rotating anode and to 2.0 A at a synchrotron source.

MeSH terms

Crystallization
Crystallography, X-Ray
Data Interpretation, Statistical
Escherichia coli / enzymology*
Oxidoreductases / chemistry*
Oxidoreductases / isolation & purification*

Substances

Oxidoreductases
3'-phosphoadenylyl-5'-phosphosulfate reductase