3IAW
Crystal structure of a chemically synthesized 203 amino acid 'covalent dimer' [Gly51;Aib51']HIV-1 protease molecule complexed with MVT-101 reduced isostere inhibitor at 1.6 A resolution
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 | 51.539, 57.988, 61.071 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.610 |
| R-factor | 0.19796 |
| Rwork | 0.197 |
| R-free | 0.22427 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.658 |
| 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 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.077 | 0.514 |
| Number of reflections | 24056 | |
| <I/σ(I)> | 39 | 6.2 |
| Completeness [%] | 98.1 | 96.9 |
| Redundancy | 9.5 | 7 |
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% (w/v) ammonium sulfate, 10% (v/v) DMSO, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
