8IQK
Structural basis of the specificity and interaction mechanism of Bmf binding to pro-survival proteins
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL02U1 |
Synchrotron site | SSRF |
Beamline | BL02U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-11-09 |
Detector | DECTRIS EIGER2 S 9M |
Wavelength(s) | 0.97918 |
Spacegroup name | P 1 2 1 |
Unit cell lengths | 102.524, 61.668, 102.528 |
Unit cell angles | 90.00, 90.19, 90.00 |
Refinement procedure
Resolution | 39.425 - 2.879 |
R-factor | 0.2285 |
Rwork | 0.226 |
R-free | 0.25500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.679 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.425 | 2.982 |
High resolution limit [Å] | 2.879 | 2.879 |
Number of reflections | 27310 | 2523 |
<I/σ(I)> | 8.92 | |
Completeness [%] | 93.0 | |
Redundancy | 6.3 | |
CC(1/2) | 0.991 | 0.655 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.2 M sodium chloride, 0.1 M sodium acetate: acetic acid, pH 4.5, 1.26 M ammonium sulfate |