3SI5
Kinetochore-BUBR1 kinase complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR-H |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-12-05 |
Detector | Bruker Platinum 135 |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 124.398, 40.143, 75.391 |
Unit cell angles | 90.00, 91.38, 90.00 |
Refinement procedure
Resolution | 38.200 - 2.200 |
R-factor | 0.19626 |
Rwork | 0.193 |
R-free | 0.24665 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2wvi |
RMSD bond length | 0.011 |
RMSD bond angle | 1.116 |
Data reduction software | SAINT |
Data scaling software | SADABS |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.200 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.119 | 0.465 |
Number of reflections | 19266 | |
<I/σ(I)> | 14.1 | 2.9 |
Completeness [%] | 99.9 | 100 |
Redundancy | 8.8 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 292 | 15% PEG 6000, 0.1M Magnesium Acetate, 0.1M Sodium Cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K |