2XFV
Structure of the amino-terminal domain from the cell-cycle regulator Swi6
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-05-01 |
| Detector | ADSC CCD |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 69.934, 69.934, 297.944 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.784 - 1.900 |
| R-factor | 0.1717 |
| Rwork | 0.171 |
| R-free | 0.19620 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.010 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.040 | 0.370 |
| Number of reflections | 35176 | |
| <I/σ(I)> | 37 | 6.8 |
| Completeness [%] | 99.4 | 100 |
| Redundancy | 10.6 | 10.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 5-15MG/ML PROTEIN, 10% PEG4000, 0.1M NA-CACODYLATE, 20MM CA-ACETATE, 0.2M NH4CL, PH 6.5 |
