7JVK
Structure of the M101A variant of the SidA ornithine hydroxylase with the FAD in the "out" conformation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2017-07-21 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 76.437, 155.275, 88.271 |
Unit cell angles | 90.00, 110.33, 90.00 |
Refinement procedure
Resolution | 56.630 - 2.200 |
R-factor | 0.1952 |
Rwork | 0.195 |
R-free | 0.22970 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 6x0h |
RMSD bond length | 0.007 |
RMSD bond angle | 0.942 |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.18) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 61.440 | 61.440 | 2.240 |
High resolution limit [Å] | 2.200 | 12.050 | 2.200 |
Rmerge | 0.108 | 0.024 | 1.235 |
Rmeas | 0.128 | 0.029 | 1.514 |
Rpim | 0.067 | 0.016 | 0.859 |
Total number of observations | 340416 | 2167 | 12230 |
Number of reflections | 96363 | 610 | 4315 |
<I/σ(I)> | 10.8 | 44.3 | 0.9 |
Completeness [%] | 98.7 | 97.9 | 89.2 |
Redundancy | 3.5 | 3.6 | 2.8 |
CC(1/2) | 0.995 | 0.990 | 0.484 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Enzyme stock solution: 8-10 mg/ml SidA (M101A) 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. Drop ratio: 2 enzyme to 1 reservoir |