8UF6
Structure of Trek-1(K2P2.1) with ML336
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-11-11 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9779 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 66.953, 118.597, 130.873 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.900 - 2.900 |
R-factor | 0.2687 |
Rwork | 0.267 |
R-free | 0.31320 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.830 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.900 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Number of reflections | 23483 | 16472 |
<I/σ(I)> | 8.7 | |
Completeness [%] | 98.0 | |
Redundancy | 7.2 | |
CC(1/2) | 0.997 | 0.209 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 277 | 20-25% PEG4000, 200 mM KCl, 100mM HEPES pH 7.0-7.5, 1mM CdCl2 |