7JX4
Crystal Structure of N-Lysine Peptoid-modified Collagen Triple Helix
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-06-05 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.7500 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 72.365, 24.756, 25.357 |
| Unit cell angles | 90.00, 98.72, 90.00 |
Refinement procedure
| Resolution | 13.620 - 0.950 |
| R-factor | 0.1407 |
| Rwork | 0.140 |
| R-free | 0.15790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1v4f |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.916 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.8.1) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 0.980 |
| High resolution limit [Å] | 0.950 | 2.050 | 0.950 |
| Rmerge | 0.096 | 0.045 | 1.147 |
| Rmeas | 0.098 | 0.046 | 1.205 |
| Rpim | 0.019 | 0.009 | 0.344 |
| Total number of observations | 580055 | ||
| Number of reflections | 24848 | 2686 | 1988 |
| <I/σ(I)> | 5.3 | ||
| Completeness [%] | 88.9 | 93.1 | 72.3 |
| Redundancy | 23.3 | 28.2 | 8.2 |
| CC(1/2) | 1.000 | 0.734 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 294 | 0.3 micor-l protein (NlysX-CMP7 [Ac-(GlyProHyp)3-GlyNlysHyp-(GlyProHyp)3]) in water at 5 mg/ml, mixed with 0.3 micro-l crystallization buffer containing 2.1 M DL-malic acid. |
