3KFR
HIV Protease (PR) dimer with inhibitor TL-3 bound and fragment 1F1 in the outside/top of flap
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 | 2008-12-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 28.720, 65.570, 92.360 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.300 - 1.300 |
| R-factor | 0.184 |
| Rwork | 0.183 |
| R-free | 0.20700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HIV PR dimer generated from monomer with TL-3 bound in 2AZ8 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.437 |
| 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] | 25.300 | 1.180 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.051 | 0.800 |
| Number of reflections | 61661 | |
| <I/σ(I)> | 6.7 | 0.9 |
| Completeness [%] | 97.8 | 96.6 |
| Redundancy | 3.8 | 3.9 |
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 |
