6EY1
prolyl hydroxylase from Trichoplax adhaerens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-24 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97930 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.579, 59.413, 51.202 |
Unit cell angles | 90.00, 100.74, 90.00 |
Refinement procedure
Resolution | 39.868 - 1.199 |
R-factor | 0.1225 |
Rwork | 0.122 |
R-free | 0.13810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2g1m |
RMSD bond length | 0.011 |
RMSD bond angle | 1.086 |
Data reduction software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.868 | 1.240 |
High resolution limit [Å] | 1.199 | 1.200 |
Rmerge | 0.084 | 0.617 |
Number of reflections | 74261 | 7022 |
<I/σ(I)> | 25.9 | 2 |
Completeness [%] | 99.4 | 94.4 |
Redundancy | 8.6 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 200nl seeded drops, 20mg/ml protein sample, 2mM MN(II)CL2, 0.2M ammonium acetate, 0.1M Bis-Tris pH 5.5, 25% PEG3350 |