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 |