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) |
