7API
THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM
Replaces: 5APIExperimental procedure
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 120.500, 120.500, 113.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 9999.000 * - 3.000 |
| R-factor | 0.193 * |
| Rwork | 0.193 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.400 |
| Refinement software | EREF |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 9999.000 * |
| High resolution limit [Å] | 3.000 * |
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 | 2.6 (M) | |
| 2 | 1 | drop | sodium phosphate | 5 (mM) | |
| 3 | 1 | drop | protein | 6-7 (mg/ml) |






