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)