4NFG
K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR591 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2010-03-01 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.890, 87.700, 104.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 67.240 - 2.110 |
| R-factor | 0.1767 |
| Rwork | 0.174 |
| R-free | 0.23614 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pcc |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.944 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 52.370 |
| High resolution limit [Å] | 2.110 |
| Number of reflections | 24499 |
| Completeness [%] | 98.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 15% PEG 3350, 150 mM NaCl, 0.5 mM 1:1 ratio of horse cytochrome c and yeast cytochrome c peroxidase, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
