4YGY
Crystal Structure of Human Scp1 bound to trans-proline peptidomimetic CTD phospho-Ser5 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-07 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03334 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 125.280, 78.335, 63.031 |
| Unit cell angles | 90.00, 112.59, 90.00 |
Refinement procedure
| Resolution | 64.860 - 2.360 |
| R-factor | 0.1862 |
| Rwork | 0.183 |
| R-free | 0.24620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.865 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.6) |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 64.860 | 50.000 | 2.400 |
| High resolution limit [Å] | 2.360 | 6.400 | 2.360 |
| Rmerge | 0.050 | 0.026 | 0.310 |
| Total number of observations | 84442 | ||
| Number of reflections | 22534 | ||
| <I/σ(I)> | 15.3 | ||
| Completeness [%] | 96.9 | 99.1 | 85.2 |
| Redundancy | 3.7 | 3.7 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 30% PEG 3350, 0.2 M magnesium acetate |
