5TSY
Structure of the glycoside hydrolase domain of PelA variant E218A from Pseudomonas aeruginosa
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER D8 QUEST |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2016-05-31 |
Detector | BRUKER PHOTON 100 |
Wavelength(s) | 1.5406 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 65.421, 84.098, 47.179 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.359 - 1.900 |
R-factor | 0.1861 |
Rwork | 0.184 |
R-free | 0.23080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5tcb |
RMSD bond length | 0.007 |
RMSD bond angle | 0.836 |
Data reduction software | SAINT |
Data scaling software | SAINT |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.084 | 0.231 |
Number of reflections | 21165 | |
<I/σ(I)> | 17 | 5.8 |
Completeness [%] | 99.8 | 100 |
Redundancy | 8.6 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 293 | 0.1 M CHES pH 9.5 and 30% (w/v) PEG 3000 |