3SAC
Crystal structure of wild-type HIV-1 protease in complex with AF80
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 | 50.880, 58.001, 61.567 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.220 - 1.500 |
| R-factor | 0.1819 |
| Rwork | 0.181 |
| R-free | 0.20380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f7a |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.445 |
| 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 | 1.550 |
| High resolution limit [Å] | 1.500 | 3.230 | 1.500 |
| Rmerge | 0.046 | 0.028 | 0.352 |
| Number of reflections | 29473 | ||
| <I/σ(I)> | 14.8 | ||
| Completeness [%] | 99.1 | 94.4 | 99.3 |
| Redundancy | 5.5 | 5.3 | 5.3 |
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 |
