3DPH
HIV-1 capsid C-terminal domain mutant (L211S)
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 1 21 1 |
| Unit cell lengths | 29.839, 74.909, 32.708 |
| Unit cell angles | 90.00, 99.98, 90.00 |
Refinement procedure
| Resolution | 37.450 - 2.010 |
| R-factor | 0.191 |
| Rwork | 0.188 |
| R-free | 0.25394 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2buo |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.941 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.4.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.400 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.094 | |
| Number of reflections | 9396 | |
| <I/σ(I)> | 27.2 | 8.9 |
| Completeness [%] | 98.9 | 91.8 |
| Redundancy | 3.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7.5 | 292 | 30% PEG4000, 100mM NaHEPES, 200mM CaCl2, pH 7.5, EVAPORATION, temperature 292K |
