2ACH
CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS
Experimental procedure
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 75.300, 75.300, 208.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.700 |
| R-factor | 0.181 * |
| Rwork | 0.181 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.680 |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 9999.000 * |
| High resolution limit [Å] | 2.700 * |
| Rmerge | 0.098 * |
| Total number of observations | 61161 * |
| Number of reflections | 14208 * |
| Completeness [%] | 79.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium potassium phosphate | 2.7 (M) | |
| 2 | 1 | drop | protein | 7 (mg/ml) | |
| 3 | 1 | drop | precipitant | 0.003 (ml) | |
| 4 | 1 | drop | phosphate | 5 (mM) |






