5ESB

Crystal structure of a genotype 1a/3a chimeric HCV NS3/4A protease in complex with Vaniprevir

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	CCD
Collection date	2014-01-14
Detector	RIGAKU SATURN 944
Wavelength(s)	1.5
Spacegroup name	P 21 21 21
Unit cell lengths	55.119, 58.403, 60.016
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.000 - 2.400
R-factor	0.1871
Rwork	0.182
R-free	0.23290
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3m5m
RMSD bond length	0.016
RMSD bond angle	1.606
Data scaling software	xia2
Phasing software	PHASER (2.5.5)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	33.300	33.300	2.460
High resolution limit [Å]	2.400	10.730	2.400
Rmerge	0.062	0.033	0.139
Number of reflections	7436
<I/σ(I)>	19.5
Completeness [%]	94.1	83.4	97
Redundancy	4.5	3.8	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	100mM MES buffer pH 6.5, 4% (w/v) ammonium sulfate, 20-26% PEG 3350