6AUJ
Crystal structure of thymidylate synthase from Elizabethkingia anophelis NUHP1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-08-07 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 144.110, 78.550, 73.370 |
Unit cell angles | 90.00, 90.49, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.700 |
R-factor | 0.1576 |
Rwork | 0.157 |
R-free | 0.17580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ix6 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.857 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.740 |
High resolution limit [Å] | 1.700 | 7.600 | 1.700 |
Rmerge | 0.056 | 0.045 | 0.576 |
Rmeas | 0.064 | 0.053 | 0.669 |
Number of reflections | 89735 | 1035 | 6648 |
<I/σ(I)> | 13.36 | 24.28 | 2.01 |
Completeness [%] | 99.7 | 96.7 | 100 |
Redundancy | 4.301 | 3.787 | 3.848 |
CC(1/2) | 0.997 | 0.993 | 0.819 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | 23.2 mg/mL ElanA.00249.a.B1.PW38270 against MORPHEUS F9 (plate id 292618f9): 10% w/v PEG20000, 20% v/v PEG550 MME, 100 mM bicine/Trizma base, pH 8.5, 20 mM D-glucose, 20 mM D-mannose, 20 mM D-galactose, 20 mM L-fucose, 20 mM D-xylose, 20 mM N-acetryl-D-glucosamine, cryoprotection: direct, puck id zfj8-8 |