6AY9
Structure of the native full-length HIV-1 capsid protein in complex with CPSF6 peptide
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 | PIXEL |
| Collection date | 2017-03-14 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.033203 |
| Spacegroup name | P 6 |
| Unit cell lengths | 92.675, 92.675, 58.042 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.030 - 2.500 |
| R-factor | 0.2438 |
| Rwork | 0.242 |
| R-free | 0.27270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xfx |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.496 |
| Data reduction software | Aimless (0.5.32) |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER (2.7.17) |
| Refinement software | PHENIX (1.11.1-2575_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.030 | 47.030 | 2.600 |
| High resolution limit [Å] | 2.500 | 9.010 | 2.500 |
| Rmerge | 0.063 | 0.033 | 0.700 |
| Rmeas | 0.069 | 0.037 | 0.774 |
| Rpim | 0.029 | 0.017 | 0.326 |
| Total number of observations | 55693 | ||
| Number of reflections | 9956 | 233 | 1119 |
| <I/σ(I)> | 18.1 | ||
| Completeness [%] | 99.9 | 99.6 | 100 |
| Redundancy | 5.6 | 5.4 | 5.5 |
| CC(1/2) | 0.998 | 0.998 | 0.583 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG3350, NaI, Sodium cacodylate, Glycerol |
