6AXS
Structure of the V11I/T58A/P122A mutant of the HIV-1 capsid protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2016-12-19 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.000032 |
Spacegroup name | P 6 |
Unit cell lengths | 92.475, 92.475, 57.675 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.076 - 2.402 |
R-factor | 0.2306 |
Rwork | 0.228 |
R-free | 0.26590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | pdbid 4XFX |
RMSD bond length | 0.004 |
RMSD bond angle | 0.633 |
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] | 36.076 | 57.680 | 2.490 |
High resolution limit [Å] | 2.400 | 8.990 | 2.400 |
Rmerge | 0.078 | 0.040 | 0.781 |
Rmeas | 0.082 | 0.042 | 0.829 |
Rpim | 0.025 | 0.014 | 0.270 |
Total number of observations | 114114 | ||
Number of reflections | 10917 | 219 | 1140 |
<I/σ(I)> | 20.7 | ||
Completeness [%] | 98.2 | 94.5 | 98.1 |
Redundancy | 10.5 | 9.9 | 8.8 |
CC(1/2) | 0.998 | 0.997 | 0.815 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG3350, NaI, Sodium cacodylate, Glycerol |