3SU5

Crystal structure of NS3/4A protease variant D168A in complex with vaniprevir

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	2010-12-07
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	55.066, 58.538, 60.015
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.010 - 1.550
R-factor	0.1657
Rwork	0.165
R-free	0.18310
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.391
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	1.610
High resolution limit [Å]	1.550	3.340	1.550
Rmerge	0.090	0.053	0.506
Number of reflections	27508
<I/σ(I)>	8.8
Completeness [%]	95.8	98.3	93
Redundancy	6.9	6.8	6.8

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