6N0W
Crystal structure of a Tyrosine--tRNA ligase from Elizabethkingia anophelis
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 | 2017-08-18 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 197.290, 37.560, 81.760 |
Unit cell angles | 90.00, 112.40, 90.00 |
Refinement procedure
Resolution | 47.957 - 2.700 |
R-factor | 0.2325 |
Rwork | 0.226 |
R-free | 0.29030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ts1 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.742 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX ((1.14_3260)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 47.957 | 47.957 | 2.770 |
High resolution limit [Å] | 2.700 | 12.080 | 2.700 |
Rmerge | 0.053 | 0.017 | 0.669 |
Rmeas | 0.060 | 0.020 | 0.746 |
Number of reflections | 15648 | 194 | 1120 |
<I/σ(I)> | 20.16 | 54.8 | 2.63 |
Completeness [%] | 99.6 | 91.9 | 100 |
Redundancy | 4.926 | 3.897 | 5.08 |
CC(1/2) | 0.999 | 0.999 | 0.905 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 287 | ElanA.01032.a.B1.PW38270 at 26 mg/mL against the Morpheus screen condition D9: 10% PEG 20,000, 20% PEG 550 MME, 0.02 M each alcohol (1,6-hexanediol, 1-butanol, R,S-1,2-propanediol, 2-propanol, 1,4-butanediol, 1,3-propanediol), 0.1 M bicine/Trizma base pH 8.5, unique puck ID xyo1-1, crystal tracking ID 292624d9 |