6EVN
Crystal structure of peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase complex with Pro-Pro-Gly-Pro-Ala-Gly-Pro-Pro-Gly.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-04-30 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 54.926, 54.926, 72.942 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.943 - 1.480 |
| R-factor | 0.1647 |
| Rwork | 0.163 |
| R-free | 0.17880 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.887 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.600 | 1.510 |
| High resolution limit [Å] | 1.480 | 1.480 |
| Rmerge | 0.051 | 0.915 |
| Rpim | 0.018 | 0.322 |
| Number of reflections | 21768 | 166 |
| <I/σ(I)> | 17.6 | 2.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.4 | 8.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 2.45 M ammonium sulphate, 10% DMSO, 5 mM PPGPAGPPG, 5% D-galactose, 100 mM MOPS, pH 6.5 |






