4A0X
Structure of the global transcription regulator FapR from Staphylococcus aureus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-11-16 |
Detector | ADSC CCD |
Spacegroup name | H 3 2 |
Unit cell lengths | 116.580, 116.580, 123.230 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 78.090 - 2.400 |
R-factor | 0.19867 |
Rwork | 0.196 |
R-free | 0.24617 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2f3x |
RMSD bond length | 0.012 |
RMSD bond angle | 1.638 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.000 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.060 | 0.630 |
Number of reflections | 12145 | |
<I/σ(I)> | 15.6 | 2.5 |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.5 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.4 | 6% PEG-8000, 0.1M MES, 0.2 M ZN ACETATE, PH 5.4 |