1FF3
STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-08-29 |
| Detector | MARRESEARCH |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 102.500, 102.500, 292.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| Rwork | 0.195 |
| R-free | 0.21800 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.330 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.035 | 0.235 |
| Total number of observations | 291810 * | |
| Number of reflections | 64402 | |
| <I/σ(I)> | 21 | |
| Completeness [%] | 88.9 | 65.6 |
| Redundancy | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | Tete-Favier, F., (2000) Acta Crystallogr. D56, 1194. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 50 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 20 (%) | |
| 3 | 1 | reservoir | ammonium sulfate | 0.35 (M) | |
| 4 | 1 | reservoir | cacodylate | 100 (mM) |
