2QVA
Crystal structure of Drosophila melanogaster Translin protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 2004-06-25 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 2 2 21 |
Unit cell lengths | 98.580, 96.620, 153.410 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.400 |
R-factor | 0.207 |
Rwork | 0.203 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2qrx |
RMSD bond length | 0.015 |
RMSD bond angle | 1.583 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.580 |
High resolution limit [Å] | 3.400 | 3.400 |
Rmerge | 0.099 | 0.354 |
Number of reflections | 18817 | |
<I/σ(I)> | 11.8 | 2.6 |
Completeness [%] | 91.4 | 77.3 |
Redundancy | 3.2 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 283 | 10% PEG 4000, 10% isopropanol, 5% glycerol, 100mM sodium citrate buffer, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 283K |