6AXT
Structure of the T58S/T107I/P122A mutant of the HIV-1 capsid protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-08 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.033760 |
| Spacegroup name | P 6 |
| Unit cell lengths | 92.407, 92.407, 57.509 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.700 - 2.400 |
| R-factor | 0.2247 |
| Rwork | 0.224 |
| R-free | 0.24330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xfx |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.474 |
| Data reduction software | Aimless (0.5.17) |
| Data scaling software | Aimless (0.5.17) |
| Phasing software | PHASER (2.5.7) |
| Refinement software | PHENIX (1.11.1-2575_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.700 | 46.700 | 2.490 |
| High resolution limit [Å] | 2.400 | 8.980 | 2.400 |
| Rmerge | 0.071 | 0.042 | 1.313 |
| Rmeas | 0.075 | 0.046 | 1.406 |
| Rpim | 0.026 | 0.016 | 0.490 |
| Total number of observations | 86620 | ||
| Number of reflections | 10448 | 205 | 1099 |
| <I/σ(I)> | 17.7 | ||
| Completeness [%] | 94.1 | 88.9 | 95.2 |
| Redundancy | 8.3 | 7.6 | 8.1 |
| CC(1/2) | 0.999 | 0.998 | 0.490 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG3350, NaI, MIB, Glycerol |
