2BTI
Structure-function studies of the RmsA CsrA post-transcriptional global regulator protein family reveals a class of RNA-binding structure
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 37.573, 37.573, 186.245 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 100.000 - 2.000 |
| R-factor | 0.224 |
| Rwork | 0.224 |
| R-free | 0.25400 |
| Structure solution method | MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.457 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.500 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.090 | 0.300 |
| Number of reflections | 9675 | |
| <I/σ(I)> | 14.8 | 4.5 |
| Completeness [%] | 98.4 | 95.1 |
| Redundancy | 6 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 0.16M AMMONIUM SULPHATE, 0.08M SODIUM ACETATE PH 4.6, 20% PEG 4000, 20% GLYCEROL, 10 MG/ML PROTEIN |
