2NXR
Structural effects of hydrophobic mutations on the active site of human carbonic anhydrase II
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 2006-01-05 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.815, 41.652, 72.933 |
Unit cell angles | 90.00, 104.67, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.700 |
Rwork | 0.181 |
R-free | 0.19910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tbt |
RMSD bond length | 0.004 |
RMSD bond angle | 1.350 |
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 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 25613 | |
Completeness [%] | 92.7 | 89.9 |
Redundancy | 3.9 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.2 | 293 | 50 mM Tris-Cl pH 8.2, 2.6 M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |