1BIX
THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 1996-12 |
Detector | RIGAKU |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.260, 44.701, 78.778 |
Unit cell angles | 90.00, 103.45, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
R-factor | 0.184 |
Rwork | 0.184 |
R-free | 0.26900 |
Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT AND ANOMALOUS SCATTERING |
RMSD bond length | 0.016 |
RMSD bond angle | 25.340 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | X-PLOR (3.84) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.310 |
High resolution limit [Å] | 2.200 | 2.190 |
Rmerge | 0.043 | 0.114 |
Total number of observations | 54729 * | |
Number of reflections | 15089 | |
<I/σ(I)> | 12.7 | 2.2 |
Completeness [%] | 98.1 | 90 |
Redundancy | 3.6 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.4 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | HEPES | 10 (mM) | |
3 | 1 | reservoir | PEG8000 | 16-20 (%(w/v)) | |
4 | 1 | reservoir | MES | 100 (mM) | |
5 | 1 | reservoir | 1,4-Dioxane | 5 (%(v/v)) | |
6 | 1 | reservoir | samarium acetate | 7.5-30 (mM) |