3DS4
HIV-1 capsid C-terminal domain mutant (L211S) in complex with an inhibitor of particle assembly (CAI)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-17 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0080 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 31.510, 69.270, 41.550 |
| Unit cell angles | 90.00, 97.66, 90.00 |
Refinement procedure
| Resolution | 35.400 - 1.120 |
| R-factor | 0.20907 |
| Rwork | 0.208 |
| R-free | 0.23412 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2buo |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.072 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.200 | 1.190 |
| High resolution limit [Å] | 1.120 | 1.120 |
| Rmerge | 0.048 | 0.410 |
| Number of reflections | 63254 | |
| <I/σ(I)> | 14.4 | 2.4 |
| Completeness [%] | 93.2 | 73.3 |
| Redundancy | 3.8 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 298 | PEG4000, 200mM ammonium sulfate, EVAPORATION, temperature 298K |
