1H2I
Human Rad52 protein, N-terminal domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 117.259, 127.319, 191.227 |
Unit cell angles | 90.00, 90.29, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.700 |
R-factor | 0.225 |
Rwork | 0.225 |
R-free | 0.26200 |
Structure solution method | MIRAS |
RMSD bond length | 0.014 |
RMSD bond angle | 1.780 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.055 | 0.279 |
Number of reflections | 149457 | |
<I/σ(I)> | 14 | 2.7 |
Completeness [%] | 97.0 | 96.7 |
Redundancy | 2.3 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | pH7.5 |
3 | 1 | drop | 300 (mM) | ||
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.0 |
6 | 1 | reservoir | ethanol | 4-14 (%(v/v)) |