8API
THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM
Replaces: 6APIExperimental procedure
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 119.700, 119.700, 216.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 9999.000 * - 3.100 |
| R-factor | 0.215 * |
| Rwork | 0.215 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.400 |
| Refinement software | EREF |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 3.100 * |
| Number of reflections | 15607 * |
| Completeness [%] | 90.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 * | 4 * | Loebermann, H., (1982) Hoppe-Seyler'S Z.Physiol. Chem., 363, 1377. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium potassium phosphate | 2.8 (M) | |
| 2 | 1 | drop | sodium phosphate | 5 (mM) | |
| 3 | 1 | drop | protein | 6-7 (mg/ml) |






