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. * |
