2AVV
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 | 2003-10-16 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.270, 62.720, 59.220 |
| Unit cell angles | 90.00, 98.15, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.500 |
| R-factor | 0.1383 |
| Rwork | 0.141 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1daz |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.027 |
| 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 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.065 | 0.239 |
| Number of reflections | 56309 | |
| <I/σ(I)> | 17.42 | 4.51 |
| Completeness [%] | 94.1 | 70.5 |
| Redundancy | 3.6 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 295 | CITRATE/PHOSPHATE BUFFER, PH 6.0, SATURATED AMMONIUM SULPHATE, 40%, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
