1EBE
Laue diffraction study on the structure of cytochrome c peroxidase compound I
Experimental procedure
Experimental method | LAUE |
Source type | SYNCHROTRON |
Source details | CHESS |
Synchrotron site | CHESS |
Temperature [K] | 279 |
Detector technology | FILM |
Collection date | 1990-11-15 |
Detector | KODAK DEF5 |
Wavelength(s) | 0.2-2.5 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 107.400, 76.800, 51.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.144 |
Rwork | 0.144 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2cyp |
RMSD bond length | 0.020 |
RMSD bond angle | 24.000 * |
Data reduction software | LEAP |
Data scaling software | LEAP |
Phasing software | CCP4 |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 8.000 |
High resolution limit [Å] | 1.600 * |
Rmerge | 0.080 * |
Total number of observations | 94847 * |
Number of reflections | 30274 * |
<I/σ(I)> | 37.5 |
Completeness [%] | 42.0 |
Redundancy | 7.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | other * | 6 | Edwards, S.L., (1987) Biochemistry, 26, 1503. * |