1JMO

Crystal Structure of the Heparin Cofactor II-S195A Thrombin Complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX14.1
Synchrotron site	SRS
Beamline	PX14.1
Temperature [K]	100
Detector technology	CCD
Collection date	2001-01-30
Detector	ADSC QUANTUM 4
Wavelength(s)	1.4880
Spacegroup name	P 61
Unit cell lengths	152.310, 152.310, 126.800
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.440 - 2.200
Rwork	0.205
R-free	0.21100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	N-terminal half of native heparin cofactor II and native S195A thrombin
RMSD bond length	0.006
RMSD bond angle	1.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.400 *	2.350
High resolution limit [Å]	2.200	2.210
Rmerge	0.080 *	0.539
Total number of observations	475985 *
Number of reflections	77117 *
<I/σ(I)>	6.5	1.5
Completeness [%]	91.1 *	62.5
Redundancy	6.2	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.4	298	NH4Cl, PEG 3350, pH 7.4, VAPOR DIFFUSION, HANGING DROP at 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	8-10 (mg/ml)
2	1	1		0.06 (M)
3	1	1	PEG3350	6 (%)