6W7X
Crystal structure of N-acetylornithine aminotransferase from Stenotrophomonas maltophilia K279a
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-03-12 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 63.820, 63.820, 172.480 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 46.530 - 1.900 |
R-factor | 0.1839 |
Rwork | 0.182 |
R-free | 0.21270 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4jev |
RMSD bond length | 0.005 |
RMSD bond angle | 0.759 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MR-Rosetta |
Refinement software | PHENIX (1.17.1) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.950 |
High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
Rmerge | 0.064 | 0.048 | 0.647 |
Rmeas | 0.068 | 0.053 | 0.714 |
Number of reflections | 33007 | 430 | 2403 |
<I/σ(I)> | 15.7 | 27.69 | 2.33 |
Completeness [%] | 99.8 | 93.3 | 99.9 |
Redundancy | 7.265 | 5.66 | 5.505 |
CC(1/2) | 0.998 | 0.995 | 0.921 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | 29.8 mg/mL StmaA.01026.b.B1.PW38742 against Molecular Dimensions Morpheus screen, condition a7 (10% w/V PEG4000, 20% V/V glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 100 mM MOPS/HEPES sodium, pH 7.5), direct cryoprotection, tray 313920a7, puck mnd6-1 |