3NJT
Crystal structure of the R450A mutant of the membrane protein FhaC
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.93340 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 107.550, 139.390, 113.080 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.560 - 3.500 |
R-factor | 0.35 |
Rwork | 0.350 |
R-free | 0.38000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gdz |
RMSD bond length | 0.013 |
RMSD bond angle | 2.200 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.600 | 3.600 |
High resolution limit [Å] | 3.500 | 3.500 |
Rmerge | 0.064 | 0.282 |
Number of reflections | 11007 | |
<I/σ(I)> | 30 | 6.1 |
Completeness [%] | 99.7 | 100 |
Redundancy | 14.5 | 14.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 28% PEG 1000, 1% B-octyl-glucoside, 500 mM imidazole pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |