8TLW
Crystal structure of MBP and AF9 AHD fusion protein 3AQA in complex with peptidomimetic inhibitor 28
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-09-22 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.12704 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 75.701, 75.701, 170.789 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.540 - 2.106 |
R-factor | 0.1794 |
Rwork | 0.176 |
R-free | 0.21320 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.900 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.4 (8-JUN-2022)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 200.000 | 200.000 | 2.140 |
High resolution limit [Å] | 2.100 | 5.700 | 2.100 |
Rmerge | 0.085 | 0.045 | 0.355 |
Rmeas | 0.088 | 0.046 | 0.366 |
Rpim | 0.021 | 0.011 | 0.085 |
Total number of observations | 501397 | ||
Number of reflections | 28836 | 1653 | 1377 |
<I/σ(I)> | 8.1 | ||
Completeness [%] | 97.2 | 97.9 | 95.5 |
Redundancy | 17.4 | 17.5 | 17.4 |
CC(1/2) | 0.999 | 0.999 | 0.982 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 20-30% PEG3350, 0.1 M Bis-Tris pH 5.5 |