4NSO
Crystal structure of the effector-immunity protein complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BSRF BEAMLINE 3W1A |
Synchrotron site | BSRF |
Beamline | 3W1A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-10 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.9793 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 133.631, 78.660, 47.860 |
Unit cell angles | 90.00, 101.52, 90.00 |
Refinement procedure
Resolution | 38.165 - 2.400 |
R-factor | 0.2199 |
Rwork | 0.215 |
R-free | 0.25900 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.048 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.073 | 0.548 |
Number of reflections | 19076 | |
<I/σ(I)> | 2.9 | |
Completeness [%] | 98.1 | |
Redundancy | 7.5 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 277 | 0.1mM HEPES pH7.6, 12%(w/v)PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 277K |