5DN4
Structure of the glycoside hydrolase domain from Salmonella typhimurium FlgJ
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2014-04-04 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.790, 43.630, 107.930 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.989 - 1.800 |
R-factor | 0.1835 |
Rwork | 0.182 |
R-free | 0.21150 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.300 |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.500 | 1.840 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.110 | 0.690 |
Number of reflections | 17650 | |
<I/σ(I)> | 12.9 | 3 |
Completeness [%] | 99.8 | 98.4 |
Redundancy | 13.3 | 12.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 35 mg/ml protein in 18-22% polyethylene glycol 3350 and 0.25-0.35 M NaI |