3RC4

Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Collection date	2010-10-28
Spacegroup name	P 21 21 21
Unit cell lengths	53.900, 58.146, 61.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	17.240 - 1.500
R-factor	0.18789
Rwork	0.186
R-free	0.21549
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3m5m
RMSD bond length	0.009
RMSD bond angle	1.280
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	20.000	20.000	1.550
High resolution limit [Å]	1.500	3.230	1.500
Rmerge	0.054	0.039	0.332
Number of reflections	27770
<I/σ(I)>	13.5
Completeness [%]	87.4	62.6	93.1
Redundancy	4.9	5.1	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	20-25% PEG 3350, 0.1M MES (pH 6.5), 4% ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K