1MUS
crystal structure of Tn5 transposase complexed with resolved outside end DNA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-D |
Synchrotron site | APS |
Beamline | 14-BM-D |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2001-12-12 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.95 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 112.700, 112.700, 235.900 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.193 |
Rwork | 0.191 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1F3I |
RMSD bond length | 0.012 |
RMSD bond angle | 2.380 |
Data reduction software | DENZO |
Data scaling software | HKL-2000 |
Phasing software | EPMR |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 61106 | |
<I/σ(I)> | 34.9 | 4.9 |
Completeness [%] | 86.7 | 61.2 |
Redundancy | 5.7 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7.7 * | 290 | Davies, D.R., (2000) Science, 289, 77. * |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | PEG-1500 | ||
2 | 1 | 1 | Hepes | ||
3 | 1 | 1 | MnCl2 | ||
4 | 1 | 1 | MgCl2 | ||
5 | 1 | 2 | MnCl2 | ||
6 | 1 | 2 | MgCl2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | 0.3 (M) | ||
2 | 1 | drop | HEPES | 20 (mM) | pH7.7 |
3 | 1 | drop | EDTA | 2 (mM) | |
4 | 1 | drop | protein | 10 (mg/ml) | |
5 | 1 | reservoir | PEG400 | 30 (%(w/v)) | |
6 | 1 | reservoir | MES | 100 (mM) | pH6.0 |
7 | 1 | reservoir | ammonium sulfate | 60 (mM) |