6EVP
Crystal structure the peptide-substrate-binding domain of human type II collagen prolyl 4-hydroxylase complexed with Pro-Pro-Gly-Pro-Glu-Gly-Pro-Pro-Gly.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-05-01 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 55.020, 55.020, 73.269 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.945 - 1.680 |
| R-factor | 0.186 |
| Rwork | 0.183 |
| R-free | 0.21510 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.974 |
| 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] | 40.000 | 1.710 |
| High resolution limit [Å] | 1.680 | 1.680 |
| Rmerge | 0.039 | 0.994 |
| Rpim | 0.014 | 0.354 |
| Number of reflections | 15052 | 765 |
| <I/σ(I)> | 21.3 | 2.1 |
| Completeness [%] | 99.6 | 99.9 |
| Redundancy | 8.2 | 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, 100 mM MOPS, 5 mM PPGPEGPPG, 5% PEG 400, 100 mM MOPS. |
