3SA3
Crystal structure of wild-type HIV-1 protease in complex with AG23
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-01-20 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.386, 57.330, 61.097 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.810 - 1.650 |
| R-factor | 0.1737 |
| Rwork | 0.172 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f7a |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.434 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.710 |
| High resolution limit [Å] | 1.650 | 3.550 | 1.650 |
| Rmerge | 0.057 | 0.035 | 0.356 |
| Number of reflections | 21177 | ||
| <I/σ(I)> | 13.2 | ||
| Completeness [%] | 96.5 | 89.8 | 97.2 |
| Redundancy | 4.9 | 4.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | HANGING DROP, VAPOR DIFFUSION | 6.2 | 295 | 24-29% ammonium sulfate, 63 mM sodium citrate, 126 mM phosphate buffer, pH 6.2, HANGING DROP, VAPOR DIFFUSION, temperature 295K |
