1FFT
The structure of ubiquinol oxidase from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-04-11 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 92.100, 372.500, 232.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 3.500 |
| R-factor | 0.446 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 3.630 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.123 | 0.399 |
| Number of reflections | 44359 | 3956 * |
| <I/σ(I)> | 7.86 | |
| Completeness [%] | 87.0 | 78.5 |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 277 | 9-10% PEG 1500, 100 mM NaCl, 100 mM MgCl2, 5% ethanol & 100 mM HEPES , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 4K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-HCl | 20 (mM) | |
| 2 | 1 | drop | OG | 1 (%) | |
| 3 | 1 | drop | protein | 20 (mg/ml) | |
| 4 | 1 | reservoir | PEG1500 | 9-10 (%(w/v)) | |
| 5 | 1 | reservoir | 100 (mM) | ||
| 6 | 1 | reservoir | 100 (mM) | ||
| 7 | 1 | reservoir | ethanol | 5 (%(v/v)) |
