2AVS
kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, and G73S
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2002-12-12 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.341, 58.431, 60.969 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.100 |
| R-factor | 0.1038 |
| Rwork | 0.107 |
| R-free | 0.14120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1daz |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.036 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.140 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.056 | 0.177 |
| Number of reflections | 72654 | |
| <I/σ(I)> | 33.81 | 5.07 |
| Completeness [%] | 98.0 | 85.9 |
| Redundancy | 6.1 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 295 | CITRATE/PHOSPHATE BUFFER, PH 5.8, SATURATED AMMONIUM SULPHATE, 30-35%, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K |
