6X0J
Structure of reduced SidA ornithine hydroxylase with the FAD "in" and complexed with NADP and L-ornithine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-02-25 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 0.979180 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 85.208, 153.015, 91.114 |
Unit cell angles | 90.00, 110.91, 90.00 |
Refinement procedure
Resolution | 56.899 - 2.335 |
R-factor | 0.1866 |
Rwork | 0.183 |
R-free | 0.24910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4b63 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.020 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.23) |
Phasing software | PHASER |
Refinement software | PHENIX (1.14) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 153.010 | 153.010 | 2.380 |
High resolution limit [Å] | 2.335 | 12.790 | 2.340 |
Rmerge | 0.198 | 0.025 | 1.372 |
Rmeas | 0.227 | 0.029 | 1.637 |
Rpim | 0.111 | 0.014 | 0.874 |
Total number of observations | 2369 | 9559 | |
Number of reflections | 90888 | 590 | 3292 |
<I/σ(I)> | 8.9 | 41.9 | 0.8 |
Completeness [%] | 98.5 | 98.9 | 71.9 |
Redundancy | 4.1 | 4 | 2.9 |
CC(1/2) | 0.984 | 0.999 | 0.352 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 293 | Enzyme stock solution: 8-10 mg/mL SidA, 1 mM NADP, and 15 mM L-Orn in 25 mM HEPES (pH 7.5) and 100 mM NaCl. Crystallization reservoir: 17-21 % PEG-3350, 0.1 M HEPES (pH 7.5), 0.1 M calcium acetate. Cryo-buffer: 15 % PEG-200, 20 % PEG 3350, 0.1 M HEPES (pH 7.5), 0.1 M calcium acetate, 100 mM NADPH and 15 mM L-Orn |