2QE7
Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2005-03-14 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.979540 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 123.210, 173.020, 218.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.997 - 3.060 |
Rwork | 0.252 |
R-free | 0.30600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmf |
RMSD bond length | 0.005 |
RMSD bond angle | 0.662 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.250 |
High resolution limit [Å] | 3.060 | 3.060 |
Rmerge | 0.119 | 0.716 |
Number of reflections | 90041 | |
<I/σ(I)> | 10.2 | 1.8 |
Completeness [%] | 91.1 | 74.9 |
Redundancy | 3.8 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 8.8 | 296 | 1M LiCl, 0.1M Tris-HCl, 20% PEG 6000 , pH 8.8, MICRO-BATCH, temperature 296K |