2YQ8
Crystal structure of the SeMet-labeled N-terminal domain and peptide substrate binding domain of alpha subunit of prolyl-4 hydroxylase type I from human.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-09-28 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 104.878, 72.017, 66.431 |
| Unit cell angles | 90.00, 91.67, 90.00 |
Refinement procedure
| Resolution | 44.622 - 2.987 |
| R-factor | 0.2124 |
| Rwork | 0.209 |
| R-free | 0.27740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v5f |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.502 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | Auto-Rickshaw |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 3.070 |
| High resolution limit [Å] | 2.990 | 2.990 |
| Rmerge | 0.080 | 0.330 |
| Number of reflections | 19064 | |
| <I/σ(I)> | 13.23 | 2.9 |
| Completeness [%] | 96.7 | 73.9 |
| Redundancy | 3.4 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 26-29% PEGMME 2000, 200MM KSCN AND 5MM DTT, 5MM SPERMINE TETRAHYDROCHLORIDE, pH 8.5 |
