1FC3
THE CRYSTAL STRUCTURE OF TRANS-ACTIVATION DOMAIN OF THE SPORULATION RESPONSE REGULATOR, SPO0A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 1999-12-10 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 43.118, 53.414, 53.718 |
Unit cell angles | 90.82, 111.73, 111.32 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.1991 |
Rwork | 0.196 |
R-free | 0.25800 |
Structure solution method | MAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.060 * | 0.313 * |
Number of reflections | 27976 | |
<I/σ(I)> | 19.41 | 3.23 |
Completeness [%] | 87.6 | 55.6 |
Redundancy | 3.6 * | 1.31 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 289 * | Muchova, K., (1999) Acta Crystallogr., D55, 671. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | reservoir | PEG4000 | 10 (%(w/v)) | |
5 | 1 | reservoir | 50 (mM) | ||
6 | 1 | reservoir | Tris-HCl | 50 (mM) |