3RC6

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 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Collection date	2010-07-21
Spacegroup name	P 21 21 21
Unit cell lengths	54.850, 58.581, 60.901
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.620 - 1.300
R-factor	0.1623
Rwork	0.161
R-free	0.19100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3m5m
RMSD bond length	0.009
RMSD bond angle	1.294
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.350
High resolution limit [Å]	1.300	2.800	1.300
Rmerge	0.048	0.032	0.377
Number of reflections	45595
<I/σ(I)>	14.8
Completeness [%]	93.1	82.8	97.1
Redundancy	4.2	4.3	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	hanging drop, vapor diffusion	6.2	295	20-25% PEG 3350, 0.1M MES (pH 6.5), 4% ammonium sulfate, hanging drop, vapor diffusion, temperature 295K