3D6W
LytTr DNA-binding domain of putative methyl-accepting/DNA response regulator from Bacillus cereus.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-03-21 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9792 |
Spacegroup name | P 42 2 2 |
Unit cell lengths | 88.784, 88.784, 74.425 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.000 - 2.400 |
R-factor | 0.184 |
Rwork | 0.182 |
R-free | 0.20900 |
Structure solution method | SAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.664 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.000 | 2.440 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.073 | 0.913 |
Number of reflections | 12166 | |
<I/σ(I)> | 13.6 | 4.4 |
Completeness [%] | 100.0 | 100 |
Redundancy | 27.8 | 26.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.4 M magnesium chloride, 0.1 M HEPES buffer. Full length protein consisting of 214 original residues was used for crystallization. The obtained crystals contain only C-terminal domain of the protein, probably, due to proteolysis of the protein in crystallization conditions. , pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |