1Z05
Crystal structure of the ROK family transcriptional regulator, homolog of E.coli MLC protein.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 32-ID |
Synchrotron site | APS |
Beamline | 32-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-02-09 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 93.719, 93.719, 118.291 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.000 |
R-factor | 0.18702 |
Rwork | 0.185 |
R-free | 0.22429 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.098 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHENIX |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.061 | 0.402 |
Number of reflections | 33945 | |
<I/σ(I)> | 52.4 | 7.9 |
Completeness [%] | 93.4 | 100 |
Redundancy | 16.5 | 14.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | 0.1M Tris-HCl, 1.5M Ammonium SO4, 12% Glycerol, 5mM beta-mercaptoethanol, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |