5HKK
Caldalaklibacillus thermarum F1-ATPase (wild type)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-02 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.873 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 147.820, 130.790, 210.390 |
Unit cell angles | 90.00, 107.97, 90.00 |
Refinement procedure
Resolution | 62.160 - 3.000 |
R-factor | 0.2051 |
Rwork | 0.203 |
R-free | 0.24610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ck3 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.567 |
Data reduction software | MOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0144) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.300 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.108 | 0.444 |
Number of reflections | 145626 | |
<I/σ(I)> | 11.6 | 3 |
Completeness [%] | 95.6 | 88.9 |
Redundancy | 3.8 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 295 | PEG 4600, PEG 1500, ADP, Magnesium chloride |