5K31
Crystal structure of Human fibrillar procollagen type I C-propeptide Homo-trimer
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-10-13 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.820, 149.630, 105.950 |
| Unit cell angles | 90.00, 101.68, 90.00 |
Refinement procedure
| Resolution | 47.070 - 2.200 |
| R-factor | 0.19767 |
| Rwork | 0.196 |
| R-free | 0.23811 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2aej |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.676 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.070 | |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.078 | |
| Number of reflections | 115206 | |
| <I/σ(I)> | 7.7 | |
| Completeness [%] | 99.8 | |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 292 | 18 % PEG 4000 and 0.1 M Tris pH 8.0 |
