8ERF
HTLV-1 capsid protein N-terminal domain orthorhombic crystal form
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 | 2022-04-08 |
Detector | DECTRIS EIGER2 S 16M |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 30.769, 77.323, 101.905 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.550 - 1.470 |
R-factor | 0.1842 |
Rwork | 0.182 |
R-free | 0.20730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Alphafold2 prediction |
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 | Inner shell | Outer shell | |
Low resolution limit [Å] | 42.550 | 42.550 | 1.490 |
High resolution limit [Å] | 1.470 | 8.030 | 1.470 |
Rmerge | 0.078 | 0.046 | 0.713 |
Rmeas | 0.081 | 0.048 | 0.744 |
Rpim | 0.023 | 0.015 | 0.210 |
Total number of observations | 553859 | 3337 | 23644 |
Number of reflections | 42553 | 324 | 1939 |
<I/σ(I)> | 15.4 | 36.4 | 2.4 |
Completeness [%] | 99.7 | 99.2 | 95.1 |
Redundancy | 13 | 10.3 | 12.2 |
CC(1/2) | 0.999 | 0.998 | 0.857 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 0.2 M (NH4)SO4, 25% PEG 4000, 0.1 M Na acetate, pH4.6 |