6FF6
Crystal structure of novel repeat protein BRIC1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-05-02 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.661, 41.953, 58.263 |
| Unit cell angles | 90.00, 90.46, 90.00 |
Refinement procedure
| Resolution | 40.840 - 2.500 |
| R-factor | 0.233 |
| Rwork | 0.229 |
| R-free | 0.27900 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.990 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | BUSTER |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.840 | 2.650 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.067 | 0.787 |
| Number of reflections | 9739 | |
| <I/σ(I)> | 12.1 | 1.67 |
| Completeness [%] | 99.7 | 98.8 |
| Redundancy | 6.55 | 6.16 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 20% v/v PEG 500 MME, 10 % w/v PEG 20,000, 30 mM MgCl2, 30 mM CaCl2 and 100 mM Tris-BICINE |
