2ICV
Kinetic and Crystallographic Studies of a Redesigned Manganese-Binding Site in Cytochrome c Peroxidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2003-01-01 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.958, 52.477, 136.250 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.600 |
R-factor | 0.223 |
Rwork | 0.223 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | : 1BES |
RMSD bond length | 0.007 |
RMSD bond angle | 1.913 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.048 | 0.302 |
Number of reflections | 34426 | |
Completeness [%] | 83.1 | 83.1 |
Redundancy | 6.1 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 277 | 1.0 M hexanediol in 0.1 M sodium acetate trihydrate, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 4.6 |