6RK9
Aspartyl/Asparaginyl beta-hydroxylase (AspH)oxygenase and TPR domains in complex with manganese, N-oxalylglycine and cyclic peptide substrate mimic of factor X
Replaces: 5JZZExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-04-04 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54 |
Spacegroup name | P 1 |
Unit cell lengths | 49.472, 59.243, 95.665 |
Unit cell angles | 103.97, 91.49, 92.70 |
Refinement procedure
Resolution | 31.997 - 2.292 |
R-factor | 0.2117 |
Rwork | 0.211 |
R-free | 0.23500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5jqy |
Data reduction software | HKL-3000 |
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 | 2.380 |
High resolution limit [Å] | 2.292 | 4.950 | 2.292 |
Rmerge | 0.150 | 0.061 | 0.992 |
Rmeas | 0.145 | 0.067 | |
Rpim | 0.069 | 0.028 | 0.466 |
Number of reflections | 46948 | 4650 | 4743 |
<I/σ(I)> | 6 | ||
Completeness [%] | 99.9 | 99.6 | 100 |
Redundancy | 5.6 | 5.8 | 5.5 |
CC(1/2) | 0.997 | 0.671 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 100 mM Bis-tris propane, 200 mM potassium thiocyanate, 20% PEG 3350, 2 mM N-oxalylglycine, 1 mM manganese chloride, 3.3 mM cyclic peptide, 18 mg/ml asph protein |