9API
THE S VARIANT OF HUMAN ALPHA1-ANTITRYPSIN, STRUCTURE AND IMPLICATIONS FOR FUNCTION AND METABOLISM
Experimental procedure
Spacegroup name | P 43 21 2 |
Unit cell lengths | 119.300, 119.300, 104.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 9999.000 * - 3.000 |
R-factor | 0.209 * |
Rwork | 0.209 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.700 |
Refinement software | EREF |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 9999.000 * |
High resolution limit [Å] | 3.000 * |
Rmerge | 0.066 * |
Total number of observations | 12963 * |
Number of reflections | 8289 * |
Completeness [%] | 47.0 * |
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 | 2.6 (M) | |
2 | 1 | drop | protein | 6-7 (mg/ml) | |
3 | 1 | drop | sodium phosphate | 5 (mM) |