3FMA
Crystal structure of the GYF domain of Smy2 in complex with a proline-rich peptide from BBP/ScSF1
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 | 2007-03-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.978522, 0.97875 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 101.400, 101.400, 150.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.057 - 2.500 |
| R-factor | 0.226 |
| Rwork | 0.225 |
| R-free | 0.25000 |
| Structure solution method | MAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.557 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | SHELXCD |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.057 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.123 | 0.878 |
| Total number of observations | 41869 | |
| Number of reflections | 27942 | |
| <I/σ(I)> | 17.8 | 2.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 15.1 | 10.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 298 | 1.2M (NH4)2SO4, 0.1M Bicine, pH 9.0, vapor diffusion, sitting drop, temperature 298K |
