1UGA
HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)
Experimental procedure
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1995-04-01 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.700, 41.700, 73.000 |
Unit cell angles | 90.00, 104.60, 90.00 |
Refinement procedure
Resolution | 6.500 - 2.000 |
R-factor | 0.154 |
Rwork | 0.154 |
R-free | 0.24600 |
Structure solution method | DIFFERENCE FOURIER |
Starting model (for MR) | NATIVE CAII HAKANSSON ET AL. 1992 |
RMSD bond length | 0.009 |
RMSD bond angle | 25.300 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 6.500 | 2.360 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.103 * | |
Total number of observations | 20445 * | |
Number of reflections | 10085 | |
<I/σ(I)> | 6.53 | 2 |
Completeness [%] | 88.1 | 89.7 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8 | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris-HCl | 50 (mM) | |
2 | 1 | drop | ammonium sulfate | 1.95-3.9 (M) | |
3 | 1 | reservoir | Tris-HCl | 50 (mM) | |
4 | 1 | reservoir | ammonium sulfate | 1.95-3.9 (M) | |
5 | 1 | drop | enzyme | ||
6 | 1 | drop | dithiothreitol | 2 (mM) |