2AVO
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 | 2003-03-05 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97105 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.465, 58.570, 61.644 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.100 |
| R-factor | 0.107 |
| Rwork | 0.108 |
| R-free | 0.13800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1daz |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.034 |
| 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 | 0.057 | 0.120 |
| Number of reflections | 75564 | |
| <I/σ(I)> | 28.23 | 7.38 |
| Completeness [%] | 98.9 | 90 |
| Redundancy | 6.1 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 295 | CITRATE/PHOSPHATE BUFFER, PH 5.2, SATURATED AMMONIUM SULPHATE, 25%, VAPOR DIFFUSION, HANGING DROP, pH 5.20, temperature 295.0K |
