2C96
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 ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-27 |
Detector | ADSC CCD |
Spacegroup name | P 65 |
Unit cell lengths | 113.027, 113.027, 39.436 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 100.000 - 1.800 |
R-factor | 0.208 |
Rwork | 0.206 |
R-free | 0.24600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bjw |
RMSD bond length | 0.027 |
RMSD bond angle | 2.102 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.1.19) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.050 | 0.370 |
Number of reflections | 26570 | |
<I/σ(I)> | 24 | 2.8 |
Completeness [%] | 97.8 | 93.5 |
Redundancy | 6 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 2M AMMONIUM FORMATE, 0.1 M HEPES PH 8.0, 5% MPD |