3O9I
Crystal Structure of wild-type HIV-1 Protease in complex with af61
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-07 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.696, 57.505, 61.769 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.110 - 1.450 |
| R-factor | 0.16981 |
| Rwork | 0.169 |
| R-free | 0.18824 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ? |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.398 |
| Data reduction software | HKL-2000 |
| 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 | 1.500 |
| High resolution limit [Å] | 1.450 | 3.120 | 1.450 |
| Rmerge | 0.047 | 0.023 | 0.330 |
| Number of reflections | 32659 | ||
| <I/σ(I)> | 13.8 | ||
| Completeness [%] | 99.8 | 98.3 | 100 |
| Redundancy | 5.1 | 4.7 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop, vapor diffusion | 6.2 | 295 | 126mM Phosphate buffer pH 6.2, 63mM Sodium Citrate, 24-29% Ammonium Sulfate, hanging drop, vapor diffusion, temperature 295K |
