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 |