4ER8
Structure of the REP associates tyrosine transposase bound to a REP hairpin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 2011-07-27 |
Detector | RIGAKU RAXIS |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 100.830, 60.300, 70.780 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.260 - 2.600 |
R-factor | 0.22781 |
Rwork | 0.225 |
R-free | 0.28136 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.930 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 23.500 | 2.670 | |
High resolution limit [Å] | 2.600 | 11.630 | 2.600 |
Rmerge | 0.040 | 0.015 | 0.565 |
Number of reflections | 25580 | ||
<I/σ(I)> | 23.46 | 65.75 | 2.23 |
Completeness [%] | 99.7 | 85.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | PEG 5000 MME, MES, 1-propanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |