4ME2
Crystal Structure of THA8 protein from Brachypodium distachyon
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-05-31 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | P 65 |
Unit cell lengths | 73.649, 73.649, 61.862 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 1.600 |
R-factor | 0.21377 |
Rwork | 0.212 |
R-free | 0.24394 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.038 |
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 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.042 | 0.883 |
Number of reflections | 25258 | |
<I/σ(I)> | 30.4 | 2.9 |
Completeness [%] | 100.0 | 100 |
Redundancy | 11.3 | 11.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 18% PEG 1500, 0.1 M HEPES, pH 7.5, 0.2 M L-Proline, VAPOR DIFFUSION, HANGING DROP, temperature 295K |