6EVO
Crystal structure the peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase complexed with Pro-Pro-Gly-Pro-Arg-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 | 55.382, 55.382, 72.994 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.962 - 1.550 |
| R-factor | 0.1602 |
| Rwork | 0.158 |
| R-free | 0.18020 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.951 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.054 | 1.035 |
| Rpim | 0.020 | 0.366 |
| Number of reflections | 19323 | 157 |
| <I/σ(I)> | 19 | 2 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 8.4 | 8.8 |
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 PPGPRGPPG, 10 mM EDTA, 100 mM MOPS |
