4S20
Structural basis for transcription reactivation by RapA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-08-17 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 336.090, 158.930, 255.010 |
Unit cell angles | 90.00, 101.28, 90.00 |
Refinement procedure
Resolution | 20.000 - 4.700 |
R-factor | 0.27829 |
Rwork | 0.273 |
R-free | 0.36926 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 4JKR & 3DMQ |
RMSD bond length | 0.007 |
RMSD bond angle | 1.101 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.530 | 4.950 |
High resolution limit [Å] | 4.700 | 4.700 |
Number of reflections | 68399 | |
<I/σ(I)> | 7.2 | 2 |
Completeness [%] | 99.4 | 99.1 |
Redundancy | 2.4 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 297 | 0.1 M HEPES, pH 7.0, 50 mM magnesium chloride, 5.2% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 297K |