1PVG
Crystal Structure of the ATPase region of Saccharomyces Cerevisiae topoisomerase II
Experimental procedure
Experimental method | MAD |
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 | 2002-05-16 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.127, 0.9796 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 58.456, 71.081, 216.132 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 * - 1.800 |
R-factor | 0.20866 |
Rwork | 0.206 |
R-free | 0.24100 * |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 0.996 * |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.061 | 0.430 |
Total number of observations | 1143715 * | |
Number of reflections | 75706 | |
<I/σ(I)> | 22 | 2.8 |
Completeness [%] | 89.5 | 72.7 |
Redundancy | 6.7 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.5 * | 4 * | PEG 1500, Potassium Chloride, Glycerol, Sodium Cacodylate, pH 6.5, microbatch under oil, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 12 (mg/ml) | |
2 | 1 | 2 | Tris-HCl | 5 (mM) | pH7.5 |
3 | 1 | 2 | 100 (mM) |