3OMA
Catalytic core subunits (I and II) of cytochrome C oxidase from Rhodobacter sphaeroides with K362M mutation
Experimental procedure
| Experimental method | SINGLE WEAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-12 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 125.019, 131.579, 176.626 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.300 |
| R-factor | 0.1922 |
| Rwork | 0.191 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.185 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.230 |
| High resolution limit [Å] | 2.150 | 4.630 | 2.150 |
| Rmerge | 0.059 | 0.029 | 0.497 |
| Number of reflections | 145094 | ||
| <I/σ(I)> | 13.8 | ||
| Completeness [%] | 92.0 | 97.6 | 57.6 |
| Redundancy | 5.5 | 6.1 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 277 | 26-28% PEG-400, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K, vapor diffusion, sitting drop |
