8FYM
Crystal structure of Fab235 in complex with MPER peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-04-26 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 |
| Unit cell lengths | 43.481, 108.300, 121.209 |
| Unit cell angles | 85.63, 82.95, 85.59 |
Refinement procedure
| Resolution | 47.950 - 2.450 |
| R-factor | 0.202 |
| Rwork | 0.200 |
| R-free | 0.24350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.484 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 2.490 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.143 | 0.811 |
| Rmeas | 0.174 | 1.000 |
| Rpim | 0.097 | 0.579 |
| Number of reflections | 78049 | 3908 |
| <I/σ(I)> | 6.96 | 1 |
| Completeness [%] | 96.3 | 96.9 |
| Redundancy | 2.9 | 2.7 |
| CC(1/2) | 0.974 | 0.386 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 1% (w/v) Tryptone, 0.05M HEPES:NaOH, 2% (v/v) PEG 400 |
