8TF7
Apo structure of protein crystal of Tri17
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-09-30 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.11583 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 105.992, 105.992, 235.824 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.340 - 2.450 |
R-factor | 0.2179 |
Rwork | 0.216 |
R-free | 0.26100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.597 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.340 | 2.530 |
High resolution limit [Å] | 2.450 | 2.450 |
Rmerge | 0.186 | 1.665 |
Rmeas | 0.191 | 1.710 |
Rpim | 0.044 | 0.388 |
Total number of observations | 937072 | 88254 |
Number of reflections | 50341 | 4566 |
<I/σ(I)> | 17.6 | 2.1 |
Completeness [%] | 100.0 | |
Redundancy | 18.6 | 19.3 |
CC(1/2) | 0.999 | 0.710 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 20% PEG3350, 100 mM KSCN, 100 mM Tris pH 8.0 |