3A5I
Structure of the cytoplasmic domain of FlhA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-06-16 |
Detector | MARRESEARCH |
Wavelength(s) | 1.00 |
Spacegroup name | I 41 |
Unit cell lengths | 216.323, 216.323, 65.070 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.800 - 2.800 |
R-factor | 0.257 |
Rwork | 0.257 |
R-free | 0.29000 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.800 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.084 | 0.398 |
Number of reflections | 37317 | |
<I/σ(I)> | 13.8 | 3 |
Completeness [%] | 99.8 | 98.8 |
Redundancy | 4.9 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 10-15% PEG300, 4-6% PEG8000, 0.1M Tris-HCl, 0.5mM EDTA, 10-15% glycerol, pH8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
2 |