3OMI
Catalytic core subunits (I and II) of cytochrome C oxidase from Rhodobacter sphaeroides with D132A 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 | 2009-11-15 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 125.064, 131.519, 175.674 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.840 - 2.150 |
R-factor | 0.193 |
Rwork | 0.192 |
R-free | 0.21500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.164 |
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 | 2.240 |
High resolution limit [Å] | 2.150 | 4.650 | 2.150 |
Rmerge | 0.092 | 0.049 | 0.556 |
Number of reflections | 151816 | ||
<I/σ(I)> | 12 | ||
Completeness [%] | 97.3 | 98.8 | 81.6 |
Redundancy | 6.9 | 7.2 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 277 | 26-29% PEG 400, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K, vapor diffusion, sitting drop |