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 |