2C9C
Structural basis of the nucleotide driven conformational changes in the AAA domain of transcription activator PspF
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 | 2005-05-04 |
Detector | ADSC CCD |
Spacegroup name | P 65 |
Unit cell lengths | 112.243, 112.243, 39.217 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 95.350 - 2.100 |
R-factor | 0.162 |
Rwork | 0.160 |
R-free | 0.19800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bjw |
RMSD bond length | 0.026 |
RMSD bond angle | 2.033 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.060 | 0.250 |
Number of reflections | 16682 | |
<I/σ(I)> | 26.7 | 4.7 |
Completeness [%] | 98.8 | 98.8 |
Redundancy | 7.9 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 2M AMMONIUM FORMATE, 0.1 M HEPES PH 8.0, 5% MPD |