1NFW

CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR XA COMPLEXED WITH RPR209685

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	1999-08-01
Detector	MARRESEARCH
Wavelength(s)	0.933
Spacegroup name	P 21 21 21
Unit cell lengths	55.950, 71.730, 78.960
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.2
Rwork	0.200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ezq
RMSD bond length	0.006
RMSD bond angle	1.270
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (98.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.100
Rmerge	0.058	0.147 *
Number of reflections	18587
Completeness [%]	96.9	98.4 *
Redundancy	2.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6 *	19 *	18-20% PEG 600, 50MM MES-NAOH,1MM RPR209685, pH 5.70 , VAPOR DIFFUSION, HANGING DROP, temperature 292 K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8 (mg/ml)
2	1	drop	MES/NaOH	5 (mM)	pH6.0
3	1	drop		5 (mM)
4	1	drop	compound 5	1000 (nM)
5	1	reservoir	PEG600	18-20 (%)
6	1	reservoir	MES/NaOH	50 (mM)	pH5.7