3ED8
Application of the superfolder YFP bimolecular fluorescence complementation for studying protein-protein interactions in vitro
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-25 |
| Detector | MAR CCD 225 mm |
| Wavelength(s) | 0.9781 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 123.040, 123.040, 247.710 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.980 - 2.700 |
| R-factor | 0.17656 |
| Rwork | 0.174 |
| R-free | 0.21774 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.852 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.980 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Number of reflections | 52991 | |
| <I/σ(I)> | 16.4 | 4.16 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 14.1 | 14.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 100 mM Tris/HCl pH 8.5, 20 % ethanol, 12 % TCEP , VAPOR DIFFUSION, HANGING DROP, temperature 293K |
