6F0W
prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation domain peptide fragment from Trichoplax adhaerens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-09-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 |
| Unit cell lengths | 40.841, 41.321, 42.076 |
| Unit cell angles | 114.06, 95.67, 103.69 |
Refinement procedure
| Resolution | 37.478 - 1.301 |
| R-factor | 0.1389 |
| Rwork | 0.138 |
| R-free | 0.16220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hqr |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.157 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.350 |
| High resolution limit [Å] | 1.300 | 2.800 | 1.300 |
| Rmerge | 0.112 | 0.065 | |
| Total number of observations | 377792 | ||
| Number of reflections | 55428 | 5723 | 5382 |
| <I/σ(I)> | 8.5 | ||
| Completeness [%] | 95.1 | 98.4 | 92.3 |
| Redundancy | 6.8 | 6.8 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 20 mg/ml protein, 1mM MN(II)CL2, 2mM N-oxalylglycine, 10mM taHIF-ODD peptide, 0.31M ammonium acetate, 24% (w/v) PEG3350, 0.1M Bis-Tris pH 5.5 |






