5K86
Aza-glycine containing collagen 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 | 2016-02-27 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 27.490, 18.240, 48.840 |
| Unit cell angles | 90.00, 91.66, 90.00 |
Refinement procedure
| Resolution | 27.478 - 1.127 |
| R-factor | 0.1319 |
| Rwork | 0.129 |
| R-free | 0.15900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3wn8 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.688 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX (dev_1370) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.480 | 1.150 |
| High resolution limit [Å] | 1.127 | 1.127 |
| Rmerge | 0.088 | 0.566 |
| Number of reflections | 18676 | |
| <I/σ(I)> | 7.1 | 1.6 |
| Completeness [%] | 99.3 | 97.7 |
| Redundancy | 2.8 | 2.4 |
| CC(1/2) | 0.995 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 277 | 0.094 M Tris-HCl (pH 7.6), 30% (w/v) PEG 4000, 0.01 M Li2SO4 monohydrate |
