4FM6
HIV-1 protease mutant V32I 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 | 2007-07-24 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.060, 86.140, 46.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.400 |
| R-factor | 0.1715 |
| Rwork | 0.172 |
| R-free | 0.23040 |
| Structure solution method | AB INITIO |
| Starting model (for MR) | 2f8g |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.029 |
| 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] | 10.000 | 1.900 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.760 | 1.400 |
| Rmerge | 0.145 | 0.425 | |
| Number of reflections | 43928 | ||
| <I/σ(I)> | 11.7 | 2.1 | |
| Completeness [%] | 98.7 | 100 | 93 |
| Redundancy | 4.9 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 0.06 M sodium acetate buffer, 0.67 M sodium chloride, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
