3FET
Crystal Structure of the Electron Transfer Flavoprotein Subunit Alpha related Protein Ta0212 from Thermoplasma acidophilum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-11-06 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.696, 115.358, 63.462 |
Unit cell angles | 90.00, 109.79, 90.00 |
Refinement procedure
Resolution | 41.490 - 2.050 |
R-factor | 0.181 |
Rwork | 0.179 |
R-free | 0.23200 |
Structure solution method | SAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.580 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.5.0053) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.090 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.104 | 0.500 |
Number of reflections | 39380 | |
<I/σ(I)> | 6.9 | 2.1 |
Completeness [%] | 95.5 | 67.6 |
Redundancy | 4.7 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 297 | 0.1 M Na Citrate pH 5.6 20% iso-Propanol, 20% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 297K |