1LQ8

Crystal structure of cleaved protein C inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2002-01-01
Detector	SBC-2
Wavelength(s)	1.0332
Spacegroup name	P 1 21 1
Unit cell lengths	55.200, 244.030, 66.400
Unit cell angles	90.00, 91.98, 90.00

Refinement procedure

Resolution	45.600 * - 2.400
Rwork	0.222
R-free	0.27900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ezx
RMSD bond length	0.008
RMSD bond angle	1.500
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.600 *	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.148	0.480
Total number of observations	68208 *
Number of reflections	55034
<I/σ(I)>	19.2	1.45
Completeness [%]	81.7 *	27.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7	293	PEG 3350, sodium fluoride, isopropanol, pH 7, VAPOR DIFFUSION, HANGING DROP at 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	drop	PEG3350	17 (%)
3	1	drop	isopropanol	3 (%)
4	1	drop		170 (mM)