1MU5
Structure of topoisomerase subunit
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-12-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.127 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 94.091, 110.968, 54.544 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.21579 |
Rwork | 0.214 |
R-free | 0.23900 * |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.313 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.058 * | 0.405 * |
Total number of observations | 284447 * | |
Number of reflections | 37738 | |
<I/σ(I)> | 16.7 | 2.65 |
Completeness [%] | 95.8 | 90.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7 | 20 * | PEG 3000, Tris, calcium acetate, pH 7.0, Microbatch, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | Tris-HCl | 20 (mM) | pH7.0 |
2 | 1 | 1 | 100 (mM) | ||
3 | 1 | 1 | protein | 12 (mg/ml) | |
4 | 1 | 2 | PEG3000 | 20 (%) | |
5 | 1 | 2 | Tris-HCl | 100 (mM) | pH7.0 |
6 | 1 | 2 | 200 (mM) |