5ETX
Crystal structure of HCV NS3/4A protease A156T variant in complex with 5172-Linear (MK-5172 linear analogue)
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 |
| Detector technology | CCD |
| Collection date | 2013-02-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.441, 63.232, 92.304 |
| Unit cell angles | 90.00, 91.65, 90.00 |
Refinement procedure
| Resolution | 27.528 - 2.350 |
| R-factor | 0.2047 |
| Rwork | 0.200 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3m5m |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.675 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.1) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 5.060 | 2.350 |
| Rmerge | 0.072 | 0.070 | 0.118 |
| Total number of observations | 129154 | ||
| Number of reflections | 31801 | ||
| <I/σ(I)> | 18.4 | ||
| Completeness [%] | 99.1 | 98.6 | 99.8 |
| Redundancy | 4.1 | 4.1 | 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 |
