1YDC
STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II
Experimental procedure
| 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 - 1.950 |
| R-factor | 0.165 |
| Rwork | 0.165 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.900 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.950 * |
| Rmerge | 0.094 * |
| Total number of observations | 19379 * |
| Number of reflections | 14137 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 0.3 (mM) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | 3 (mM) | ||
| 4 | 1 | reservoir | Tris-HCl | 50 (mM) | |
| 5 | 1 | reservoir | 3 (mM) | ||
| 6 | 1 | reservoir | ammonium sulfate | 1.75-2.5 (M) |
