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 |
