1MOO
Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-08-04 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.938 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.188, 41.435, 72.041 |
Unit cell angles | 90.00, 104.26, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.050 |
R-factor | 0.158 |
Rwork | 0.157 |
R-free | 0.17700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 0.030 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 1.050 | 1.050 * |
Rmerge | 0.106 | 0.316 * |
Number of reflections | 93527 * | 4547 * |
Completeness [%] | 83.1 | 40.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 277 | Duda, D., (2001) Protein Pept. Lett., 8, 63. * |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 277 | Duda, D., (2001) Protein Pept. Lett., 8, 63. * |