3KFP
HIV Protease (PR) with inhibitor TL-3 bound, and DMSOs in exo site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 62.390, 62.390, 82.060 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.670 - 1.770 |
| R-factor | 0.22969 |
| Rwork | 0.226 |
| R-free | 0.31318 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HIV Protease monomer in 2AZ8 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.987 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0090) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.030 | 1.810 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.099 | 0.734 |
| Number of reflections | 9561 | |
| <I/σ(I)> | 4.1 | 0.8 |
| Completeness [%] | 98.4 | 98.1 |
| Redundancy | 6.5 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.8 | 277 | 0.5 M KSCN, 0.1 M MES-HCL, pH 5.8, 10% DMSO, VAPOR DIFFUSION, temperature 277K |
