9HPQ
Peptide-substrate-binding (PSB) domain of human type I 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 MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-09-29 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 82.418, 86.315, 91.132 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.880 - 2.170 |
| Rwork | 0.225 |
| R-free | 0.24990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.525 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.880 | 2.250 |
| High resolution limit [Å] | 2.170 | 2.170 |
| Rmerge | 0.058 | 1.412 |
| Number of reflections | 34940 | 3373 |
| <I/σ(I)> | 13.5 | 1.1 |
| Completeness [%] | 99.6 | 99.6 |
| Redundancy | 4.7 | 4.7 |
| CC(1/2) | 0.999 | 0.482 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 278 | 30% MPD, 50 mM MgCl2, 50 mM KCl, 100 mM MOPS |
