4LEU
Crystal Structure of THA8-like protein from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-11-28 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 117.170, 53.302, 42.312 |
Unit cell angles | 90.00, 99.69, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.20659 |
Rwork | 0.204 |
R-free | 0.25306 |
Structure solution method | SAD |
RMSD bond length | 0.015 |
RMSD bond angle | 1.391 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELX |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.072 | 0.839 |
Number of reflections | 17384 | |
<I/σ(I)> | 15.3 | 2 |
Completeness [%] | 99.2 | 95.1 |
Redundancy | 7.2 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 295 | 12% (w/v) PEG3350, 4% (v/v) Tacsimate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |