4M2R
Human Carbonic Anhydrase II in complex with Brinzolamide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2012-09-30 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.837, 42.163, 72.643 |
| Unit cell angles | 90.00, 104.76, 90.00 |
Refinement procedure
| Resolution | 19.083 - 1.993 |
| R-factor | 0.1738 |
| Rwork | 0.172 |
| R-free | 0.21580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.377 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.070 |
| High resolution limit [Å] | 1.993 | 2.000 |
| Number of reflections | 16312 | |
| Completeness [%] | 94.9 | 97.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Drops were prepared by mixing 7 uL of the final concentrated protein (~10 mg/mL) and 3uL of precipitant solution against 1 mL of precipitant solution. The precipitant solution conditions varied, and consisted of 50 mM Tris-HCl (pH 7.5) and 1.6 M sodium citrate, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
