5DN5
Structure of a C-terminally truncated 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 | 2014-06-16 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 105.700, 61.120, 65.220 |
Unit cell angles | 90.00, 106.70, 90.00 |
Refinement procedure
Resolution | 29.756 - 2.150 |
R-factor | 0.1789 |
Rwork | 0.175 |
R-free | 0.25170 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.409 |
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] | 37.470 | 2.220 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.150 | 0.830 |
Number of reflections | 21763 | |
<I/σ(I)> | 10.3 | 2.5 |
Completeness [%] | 99.7 | 99 |
Redundancy | 7.3 | 7.3 |
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 |