8TMV
HTLV-1 capsid protein N-terminal domain triclinic crystal form with phosphate ion
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-04-18 |
Detector | DECTRIS EIGER2 X 16M |
Wavelength(s) | 0.95372 |
Spacegroup name | P 1 |
Unit cell lengths | 28.195, 30.720, 36.081 |
Unit cell angles | 65.19, 79.30, 89.56 |
Refinement procedure
Resolution | 27.800 - 1.730 |
R-factor | 0.2015 |
Rwork | 0.200 |
R-free | 0.22980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 8ere |
RMSD bond length | 0.003 |
RMSD bond angle | 0.588 |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHASER (2.8.3) |
Refinement software | PHENIX (1.20.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.080 | 1.670 |
High resolution limit [Å] | 1.640 | 1.640 |
Rmerge | 0.067 | 1.007 |
Rmeas | 0.079 | 1.203 |
Rpim | 0.042 | 0.648 |
Total number of observations | 43879 | 1657 |
Number of reflections | 12672 | 532 |
<I/σ(I)> | 6.2 | 0.7 |
Completeness [%] | 95.9 | |
Redundancy | 3.5 | 3.1 |
CC(1/2) | 0.998 | 0.456 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 10% ethylene glycol, 10% PEG 8K, 0.1 M HEPES, pH 7.5 |