Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1

Katia D'Ambrosio; Giuseppina De Simone; Emilia Pedone; Mosè Rossi; Simonetta Bartolucci; Carlo Pedone

doi:10.1107/S1744309105004057

Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt 3):335-6. doi: 10.1107/S1744309105004057. Epub 2005 Mar 1.

Authors

Katia D'Ambrosio¹, Giuseppina De Simone, Emilia Pedone, Mosè Rossi, Simonetta Bartolucci, Carlo Pedone

Affiliation

¹ Dipartimento di Chimica Biologica-Sezione Biostrutture, Istituto di Biostrutture e Bioimmagini-CNR, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.

Abstract

A protein disulfide oxidoreductase from the archaeon Aeropyrum pernix K1 has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to the space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 90.59, b = 102.43, c = 128.96 A. A complete data set has been collected at the Elettra synchrotron source in Trieste to 1.93 A resolution using a single frozen crystal.

MeSH terms

Aeropyrum / enzymology*
Archaeal Proteins / chemistry
Archaeal Proteins / genetics
Archaeal Proteins / isolation & purification
Cloning, Molecular
Crystallization
Escherichia coli / enzymology
Oxidoreductases Acting on Sulfur Group Donors / chemistry*
Oxidoreductases Acting on Sulfur Group Donors / isolation & purification
Recombinant Proteins / chemistry
Recombinant Proteins / isolation & purification
X-Ray Diffraction

Substances

Archaeal Proteins
Recombinant Proteins
Oxidoreductases Acting on Sulfur Group Donors