1ULY
Crystal structure analysis of the ArsR homologue DNA-binding protein from P. horikoshii OT3
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-06-27 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9792, 0.9795, 0.9685 |
Spacegroup name | H 3 2 |
Unit cell lengths | 90.640, 90.640, 132.260 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.500 |
Rwork | 0.204 |
R-free | 0.26800 |
Structure solution method | MAD |
RMSD bond length | 0.004 |
RMSD bond angle | 0.900 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.083 | 0.295 |
Number of reflections | 7284 | |
<I/σ(I)> | 8 | |
Completeness [%] | 99.4 | 99.4 |
Redundancy | 10.5 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | PEG400, HEPES, magnesium chloride, glycerol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |