6X0H
Structure of oxidized SidA ornithine hydroxylase with the FAD in the "out" conformation
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 | 76.765, 156.937, 88.651 |
Unit cell angles | 90.00, 110.38, 90.00 |
Refinement procedure
Resolution | 65.411 - 2.087 |
R-factor | 0.1849 |
Rwork | 0.182 |
R-free | 0.23220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4b63 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.919 |
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] | 156.940 | 156.940 | 2.120 |
High resolution limit [Å] | 2.087 | 11.430 | 2.090 |
Rmerge | 0.110 | 0.025 | 0.858 |
Rmeas | 0.142 | 0.032 | 1.113 |
Rpim | 0.088 | 0.020 | 0.702 |
Total number of observations | 1659 | 10926 | |
Number of reflections | 114542 | 696 | 5054 |
<I/σ(I)> | 6 | 17.6 | 1 |
Completeness [%] | 98.4 | 95.4 | 87.4 |
Redundancy | 2.3 | 2.4 | 2.2 |
CC(1/2) | 0.991 | 0.997 | 0.416 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 293 | Enzyme stock solution: 8-10 mg/mL SidA 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 |