5DF5
The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2013-06-22 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.07812 |
Spacegroup name | P 1 |
Unit cell lengths | 34.609, 51.739, 61.748 |
Unit cell angles | 110.01, 93.09, 91.88 |
Refinement procedure
Resolution | 57.880 - 1.301 |
R-factor | 0.14949 |
Rwork | 0.148 |
R-free | 0.17771 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5c0z |
RMSD bond length | 0.018 |
RMSD bond angle | 1.884 |
Data reduction software | XDS (September 26, 2012) |
Data scaling software | Aimless (0.1.29) |
Phasing software | PHENIX (1.8.1) |
Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.881 | 1.335 |
High resolution limit [Å] | 1.301 | 1.301 |
Rmerge | 0.081 | 0.504 |
Number of reflections | 90455 | |
<I/σ(I)> | 15.3 | 2.6 |
Completeness [%] | 96.6 | 89.38 |
Redundancy | 5.3 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 295 | 20 mg/mL protein in water mixed 1:1 with 30% PEG 1500 |