2OC1

Structure of the HCV NS3/4A Protease Inhibitor CVS4819

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Wavelength(s)	1.5418
Spacegroup name	H 3 2
Unit cell lengths	222.936, 222.936, 75.158
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.700
Rwork	0.189
R-free	0.25900
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	2o8m
RMSD bond length	0.008
RMSD bond angle	1.790
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (98.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.800
High resolution limit [Å]	2.700	2.700
Number of reflections	19837
<I/σ(I)>	23.3	3.3
Completeness [%]	99.7	99.8
Redundancy	3.6	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	277	The protein (NS3 complexed with KK-NS4a(21-39)-KK peptide) was at 12-15 mg/ml in 15 mM MES, pH 6.5 1 M NaCl 20 mM b-mercaptoethanol. Hanging Drops were formed by mixing 4:l protein solution with 4:l {0.75-1.0 M NaCl 0.1M Na/K phosphate 0.1 M Mes, pH 5.8-6.1 20 mM b -mercaptoethanol} The drop was equilibrated the drops over 1 ml {(1.25-1.50 M) NaCl - 0.1M Na/K phosphate 0.1 M Mes, pH 5.6-5.8, 20 mM b-mercaptoethanol} , VAPOR DIFFUSION, HANGING DROP, temperature 277K