5EPN
Crystal structure of HCV NS3/4A protease in complex with 5172-mcP1P3 (MK-5172 P1-P3 macrocyclic analogue)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-03-08 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.5 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.300, 58.510, 60.130 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.300 |
R-factor | 0.1542 |
Rwork | 0.152 |
R-free | 0.19930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3m5m |
Data reduction software | xia2 |
Data scaling software | xia2 |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 40.000 |
High resolution limit [Å] | 2.300 |
Number of reflections | 8436 |
<I/σ(I)> | 9 |
Completeness [%] | 99.9 |
Redundancy | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 20 to 26% PEG-3350, 0.1 M sodium MES buffer at pH 6.5, and 4% ammonium sulfate |