5VSG
Fibrils of the super helical repeat peptide, SHR-FF, grown at elevated temperature
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 | PIXEL |
| Collection date | 2017-03-05 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 5.343, 20.883, 16.795 |
| Unit cell angles | 90.00, 93.90, 90.00 |
Refinement procedure
| Resolution | 16.760 - 1.100 |
| R-factor | 0.1169 |
| Rwork | 0.114 |
| R-free | 0.13420 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.827 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 100.000 | 20.883 | 1.140 |
| High resolution limit [Å] | 1.100 | 2.370 | 1.100 |
| Rmerge | 0.165 | 0.123 | 0.308 |
| Total number of observations | 4946 | ||
| Number of reflections | 1367 | ||
| <I/σ(I)> | 6.5 | ||
| Completeness [%] | 89.2 | 97 | 53.5 |
| Redundancy | 3.6 | 4.2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 7.4 | 310 | 5% DMSO, 100 mM HEPES |
