2R9G
Crystal structure of the C-terminal fragment of AAA ATPase from Enterococcus faecium
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-08-31 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 1 |
Unit cell lengths | 82.778, 103.390, 103.374 |
Unit cell angles | 90.01, 88.69, 86.05 |
Refinement procedure
Resolution | 20.000 - 2.090 |
R-factor | 0.199 |
Rwork | 0.197 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2qw6 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.151 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.3.0034) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.180 |
High resolution limit [Å] | 2.090 | 2.090 |
Rmerge | 0.126 | 0.760 |
Number of reflections | 202788 | |
<I/σ(I)> | 2.8 | 2.1 |
Completeness [%] | 87.3 | 44.4 |
Redundancy | 3.6 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 294 | 100mM HEPES pH 7.5, 25% PEG 3350, 200mM Ammonium acetate, temperature 294K |