4YH1
Structure of Human Scp1 bound to cis-proline peptidomimetic CTD phospho-Ser5 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-04-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97648 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 125.115, 78.804, 62.853 |
| Unit cell angles | 90.00, 112.54, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.200 |
| R-factor | 0.1953 |
| Rwork | 0.193 |
| R-free | 0.24630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.002 |
| Data reduction 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] | 50.000 | 50.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 5.970 | 2.200 |
| Rmerge | 0.110 | 0.033 | 0.495 |
| Total number of observations | 101636 | ||
| Number of reflections | 27838 | ||
| <I/σ(I)> | 6.3 | ||
| Completeness [%] | 97.0 | 99.6 | 83 |
| Redundancy | 3.7 | 3.8 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 30% PEG 3350, 0.2 M magnesium acetate |
