8SM5
Crystal Structure of BHRF1 from Epstein Barr Virus in complex with BID BH3 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-10-17 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.979180 |
Spacegroup name | P 65 |
Unit cell lengths | 186.817, 186.817, 70.486 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 80.894 - 2.610 |
R-factor | 0.200666449516 |
Rwork | 0.198 |
R-free | 0.25966 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.193 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 161.790 | 2.710 |
High resolution limit [Å] | 2.610 | 2.610 |
Number of reflections | 42919 | 4267 |
<I/σ(I)> | 19.6 | |
Completeness [%] | 99.9 | |
Redundancy | 11.3 | |
CC(1/2) | 0.998 | 0.611 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 277.15 | 0.1 mM NaC2H3O2 pH 5.0, 1.6 mM HCOONa |