3FG7
The crystal structure of villin domain 6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-31 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 31 |
| Unit cell lengths | 47.820, 47.820, 98.173 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 23.910 - 2.000 |
| R-factor | 0.19961 |
| Rwork | 0.197 |
| R-free | 0.24622 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1p8x |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.499 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.048 | 0.282 |
| Number of reflections | 16865 | |
| Completeness [%] | 99.6 | 98.8 |
| Redundancy | 4.8 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | The protein(10mg/ml)was mixed in a 1:1 ratio(v/v)with a reservoir solution containing 15%(w/v)PEG8000, 100mM NaOAc buffer, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277KK |
