2EFL
Crystal structure of the EFC domain of formin-binding protein 17
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-14 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 200.985, 41.397, 56.467 |
| Unit cell angles | 90.00, 105.12, 90.00 |
Refinement procedure
| Resolution | 42.100 - 2.610 |
| R-factor | 0.212 |
| Rwork | 0.212 |
| R-free | 0.26700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2efk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.000 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.101 | 0.260 |
| Number of reflections | 12632 | |
| <I/σ(I)> | 17.1 | 4.6 |
| Completeness [%] | 90.8 | 62.3 |
| Redundancy | 5.9 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 15% Isopropanol, 20mM magnesium chloride, 50mM MES-NaOH, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
