3DS1
HIV-1 capsid C-terminal domain mutant (E187A) in complex with an inhibitor of particle assembly (CAI)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-25 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.044 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 42.894, 42.894, 90.813 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.170 - 1.600 |
| R-factor | 0.21501 |
| Rwork | 0.212 |
| R-free | 0.27222 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2buo |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.357 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.4.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.800 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.043 | 0.368 |
| Number of reflections | 11802 | |
| <I/σ(I)> | 73.8 | 9.7 |
| Completeness [%] | 99.7 | 98.6 |
| Redundancy | 3.6 | 19.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 4.2 | 298 | 30% PEG 4000, 100mM ammonium acetate, 10mM MgCl2, pH 4.2, EVAPORATION, temperature 298.0K |
