2AVQ
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 | MAR CCD 165 mm |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 57.886, 85.969, 46.503 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.300 |
| Rwork | 0.111 |
| R-free | 0.14410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB Enrty 1DAZ |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.030 |
| 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 | 1.350 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.058 | 0.281 |
| Number of reflections | 57183 | |
| <I/σ(I)> | 26.79 | 4.14 |
| Completeness [%] | 92.2 | 93.9 |
| Redundancy | 6.7 | 3.3 |
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, 15-20%,DMSO 10%, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K |
