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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | D'Ambrosio, Katia De Simone, Giuseppina Pedone, Emilia Rossi, Mosè Bartolucci, Simonetta Pedone, Carlo |
| Description | Country affiliation: Italy Author Affiliation: D'Ambrosio K ( 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. |
| File Format | HTM / HTML |
| ISSN | 2053230X |
| e-ISSN | 17443091 |
| Journal | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
| Issue Number | Pt 3 |
| Volume Number | 61 |
| Language | English |
| Publisher | Wiley |
| Publisher Date | 2005-03-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Aeropyrum Enzymology Oxidoreductases Acting On Sulfur Group Donors Chemistry Archaeal Proteins Genetics Isolation & Purification Cloning, Molecular Crystallization Escherichia Coli Recombinant Proteins X-ray Diffraction |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics |
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