4OCH
Apo structure of Smr domain of MutS2 from Deinococcus radiodurans
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-02 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97930 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 24.980, 47.510, 30.810 |
| Unit cell angles | 90.00, 99.52, 90.00 |
Refinement procedure
| Resolution | 25.598 - 1.400 |
| R-factor | 0.1937 |
| Rwork | 0.192 |
| R-free | 0.22060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.776 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.670 | 1.440 |
| High resolution limit [Å] | 1.400 | 1.620 | 1.400 |
| Rmerge | 0.070 | 0.700 | |
| Number of reflections | 13788 | ||
| <I/σ(I)> | 14.02 | 2.39 | |
| Completeness [%] | 98.1 | 99.3 | 97.8 |
| Redundancy | 3.6 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | crystal formed spontaneously in protein solution stored at 4 degree | 8.8 | 297 | 30mM NaCl and 20mM Tris-HCl, pH 8.8, crystal formed spontaneously in protein solution stored at 4 degree, temperature 297K |
