4Z1R
Crystal structure of collagen-like peptide at 1.27 Angstrom resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-11-13 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 0.91841 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 171.573, 13.939, 24.981 |
| Unit cell angles | 90.00, 94.59, 90.00 |
Refinement procedure
| Resolution | 28.500 - 1.270 |
| R-factor | 0.1396 |
| Rwork | 0.137 |
| R-free | 0.17130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cag |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.031 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.350 |
| High resolution limit [Å] | 1.270 | 3.790 | 1.270 |
| Rmerge | 0.052 | 0.035 | 0.148 |
| Rmeas | 0.060 | 0.041 | 0.179 |
| Total number of observations | 60616 | ||
| Number of reflections | 16057 | 663 | 2387 |
| <I/σ(I)> | 17.15 | 27.22 | 8.01 |
| Completeness [%] | 98.6 | 95.3 | 93.7 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 292 | 20% PEG 400, 5% acetic acid |
