4FLG
HIV-1 protease mutant I47V complexed with reaction intermediate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-16 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.080, 86.300, 46.350 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.310 |
| R-factor | 0.1442 |
| Rwork | 0.142 |
| R-free | 0.17970 |
| Structure solution method | AB INITIO PHASING |
| Starting model (for MR) | 1fg6 |
| RMSD bond length | 0.031 |
| RMSD bond angle | 0.039 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.780 | 1.360 |
| High resolution limit [Å] | 1.310 | 1.650 | 1.310 |
| Rmerge | 0.140 | 0.601 | |
| Number of reflections | 53227 | ||
| <I/σ(I)> | 16.9 | 2.1 | |
| Completeness [%] | 98.8 | 100 | 98.8 |
| Redundancy | 7.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 298 | 0.05 M sodium acetate buffer, 1.2 M sodium formate, and 2.5% PEG8000, pH 5.0, temperature 298K |
