1IZ2

Interactions causing the kinetic trap in serpin protein folding

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 6B
Synchrotron site	PAL/PLS
Beamline	6B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-06-20
Detector	MACSCIENCE
Wavelength(s)	1.1
Spacegroup name	P 21 21 21
Unit cell lengths	63.020, 74.173, 93.115
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 2.200
R-factor	0.221
Rwork	0.211
R-free	0.27900 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008 *
RMSD bond angle	1.333 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000 *
High resolution limit [Å]	2.200	2.200
Rmerge	0.059 *	0.253 *
Number of reflections	21991 *	2115 *
Completeness [%]	96.6 *	94.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6 *	22 *	Ammonium Sulfate 1.8M, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	ammonium sulfate	1.8 (M)
2	1	drop	sodium potassium tartrate	0.2 (M)
3	1	drop	sodium citrate	0.1 (M)	pH5.6
4	1	drop	n-octanol-sucrose	5 (%)
5	1	drop	protein	12 (mg/ml)