7BBQ
Crystal structure of the HTH DNA binding protein ArdK from R388 plasmid. Apo form.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM16 |
Synchrotron site | ESRF |
Beamline | BM16 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2007-04-19 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9794 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 43.100, 43.100, 190.890 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.100 - 3.000 |
R-factor | 0.2478 |
Rwork | 0.246 |
R-free | 0.27080 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.442 |
Data reduction software | MOSFLM (7.2.2) |
Data scaling software | SCALA (CCP4 7.0.078) |
Phasing software | PHENIX (1.17.1_3660) |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 63.630 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.097 | 0.371 |
Rmeas | 0.112 | 0.428 |
Number of reflections | 4103 | 565 |
<I/σ(I)> | 11.3 | 3.8 |
Completeness [%] | 99.8 | |
Redundancy | 6.6 | |
CC(1/2) | 0.992 | 0.963 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | 20 mM Tris-HCl, 150 mM NaCl, 1 mM EDTA |