5EPY

Crystal structure of HCV NS3/4A protease A156T variant in complex with 5172-mcP1P3 (MK-5172 P1-P3 macrocyclic analogue)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-03-14
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 21 21 21
Unit cell lengths	54.994, 58.440, 60.089
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 - 2.300
R-factor	0.1756
Rwork	0.173
R-free	0.21670
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3m5m
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.000	35.000	2.380
High resolution limit [Å]	2.300	4.950	2.300
Rmerge	0.068	0.043	0.200
Total number of observations	39511
Number of reflections	9070
<I/σ(I)>	9.1
Completeness [%]	100.0	100	100
Redundancy	4.4	4	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