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 |