3HZC
Crystal structure of a chemically synthesized 203 amino acid 'covalent dimer' [Gly51;Aib51']HIV-1 protease molecule complexed with MVT-101 reduced isostere inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2006-08-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97932 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 51.532, 57.964, 61.015 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.450 |
| R-factor | 0.20523 |
| Rwork | 0.203 |
| R-free | 0.24446 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fsm |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.657 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.500 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.083 | 0.598 |
| Number of reflections | 30346 | |
| <I/σ(I)> | 25.4 | 2.46 |
| Completeness [%] | 92.7 | 61.1 |
| Redundancy | 6.2 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 0.1M citrate, 0.2M sodium phosphate, 30% (w/v) ammonium sulfate, 10% (v/v) DMSO, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
