3DS5
HIV-1 capsid C-terminal domain mutant (N183A)
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 |
| Unit cell lengths | 51.359, 51.321, 51.358 |
| Unit cell angles | 109.20, 109.63, 109.55 |
Refinement procedure
| Resolution | 41.960 - 2.400 |
| R-factor | 0.22269 |
| Rwork | 0.220 |
| R-free | 0.26977 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a80 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.617 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.025 | 0.139 |
| Number of reflections | 13571 | |
| <I/σ(I)> | 36.4 | 5 |
| Completeness [%] | 86.3 | 43.6 |
| Redundancy | 3.1 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 4.6 | 298 | 30% PEG 4000, 100mM ammonium acetate, 10mM MgCl2, pH 4.6, EVAPORATION, temperature 298.0K |
