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 |