4GEQ
Crystal structure of the Spc24-Spc25/Cnn1 binding interface
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P13 (MX1) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-10-02 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.127 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.142, 61.848, 139.056 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.090 - 2.010 |
R-factor | 0.2092 |
Rwork | 0.207 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ftx |
RMSD bond length | 0.010 |
RMSD bond angle | 0.970 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 61.850 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.113 | 0.577 |
Number of reflections | 19858 | |
<I/σ(I)> | 8.5 | 2.5 |
Completeness [%] | 96.9 | 87.1 |
Redundancy | 4.6 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 293.15 | 15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |