2C99
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 | 113.250, 113.250, 39.332 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 100.000 - 1.900 |
R-factor | 0.166 |
Rwork | 0.164 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bjw |
RMSD bond length | 0.021 |
RMSD bond angle | 1.951 |
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 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.050 | 0.320 |
Number of reflections | 22409 | |
<I/σ(I)> | 22.7 | 2.9 |
Completeness [%] | 97.6 | 92.4 |
Redundancy | 6 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 2M AMMONIUM FORMATE, 0.1 M HEPES PH 8.0, 5% MPD |