3RRW
Crystal structure of the TL29 protein from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-06 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97926 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 92.350, 92.350, 143.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.170 - 2.500 |
R-factor | 0.22753 |
Rwork | 0.225 |
R-free | 0.27550 |
Structure solution method | SAD |
RMSD bond length | 0.015 |
RMSD bond angle | 1.336 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHENIX |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.280 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.092 | 0.346 |
Number of reflections | 22173 | |
<I/σ(I)> | 4.3 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.2 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 291 | Reservoir solution: 16 % PEG 4000, 0.2M potassium phosphate, 10 % glycerol. Protein solution: 16 mM sodium phosphate, 0.1 M NaCl, 10 % glycerol, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K |