1N1L

CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND INHIBITOR (GW472467X)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	H 3 2
Unit cell lengths	225.450, 225.450, 75.890
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.600
R-factor	0.18508
Rwork	0.183
R-free	0.22000 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.741
Data reduction software	DENZO
Data scaling software	CCP4 ((TRUNCATE))
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.690
High resolution limit [Å]	2.600	2.600
Rmerge	0.052	0.238
Number of reflections	21878
<I/σ(I)>	16.6	4.5
Completeness [%]	96.3	92

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	Kim, J.L., (1996) 8, 344. *