3HHG
Structure of CrgA, a LysR-type transcriptional regulator from Neisseria meningitidis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9765 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 104.638, 119.091, 250.204 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.880 - 3.200 |
| R-factor | 0.21787 |
| Rwork | 0.214 |
| R-free | 0.28584 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hhf |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.931 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0047) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.061 | 0.512 |
| Number of reflections | 43934 | |
| <I/σ(I)> | 17.8 | 1.66 |
| Completeness [%] | 83.8 | 85.3 |
| Redundancy | 3.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | 10% v/v MPD, 0.1M sodium acetate pH5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
