3KA2
Crystal structure of chemically synthesized 203 amino acid 'covalent dimer' [L-Ala;Gly51']HIV-1 protease molecule complexed with MVT-101 reduced isostere inhibitor at 1.4 A resolution
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] | 110 |
| Detector technology | CCD |
| Collection date | 2007-02-26 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.90020 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.695, 58.074, 61.593 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.400 |
| R-factor | 0.19751 |
| Rwork | 0.196 |
| R-free | 0.21728 |
| Structure solution method | Molrep v.5 |
| Starting model (for MR) | 3hau |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.731 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP (v.5) |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.450 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.068 | 0.437 |
| Number of reflections | 36259 | |
| <I/σ(I)> | 25.46 | 2.85 |
| Completeness [%] | 98.4 | 93 |
| Redundancy | 6.4 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 0.1 M CITRATE, 0.2 M SODIUM PHOSPHATE, 30% (V/V) AMMONIUM SULFATE, 10% (V/V) DMSO, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
