6RJP
Bfl-1 in complex with alpha helical peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-01-31 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.975312 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 113.749, 113.749, 79.148 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.570 |
| R-factor | 0.2025 |
| Rwork | 0.199 |
| R-free | 0.26590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vm6 |
| Data reduction software | XDS |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | BUSTER |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 61.700 | 2.940 |
| High resolution limit [Å] | 2.570 | 2.570 |
| Rmerge | 0.046 | 0.685 |
| Rmeas | 0.051 | 0.776 |
| Rpim | 0.027 | 0.359 |
| Number of reflections | 10669 | 533 |
| <I/σ(I)> | 13.3 | |
| Completeness [%] | 55.5 | |
| Redundancy | 3.6 | |
| CC(1/2) | 0.999 | 0.692 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | 0.1 M sodium acetate pH 4.6 16% (w/v) PEG smear high |






