3K2Z
Crystal structure of a LexA protein from Thermotoga maritima
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-13 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 116.770, 62.676, 57.017 |
| Unit cell angles | 90.00, 98.98, 90.00 |
Refinement procedure
| Resolution | 13.510 - 1.370 |
| R-factor | 0.205 |
| Rwork | 0.203 |
| R-free | 0.23100 |
| Structure solution method | SAD |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.286 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 25.000 |
| High resolution limit [Å] | 1.370 |
| Number of reflections | 85313 |
| <I/σ(I)> | 21.2 |
| Redundancy | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | hanging drop | 6.8 | 292 | 0.1M Bis-tris propane, 0.4M ammonium sulfate, 10% glycerol, pH 6.8, hanging drop, temperature 292K |
