7AQV
Flavin-dependent tryptophan halogenase Thal: N-terminally His-tagged form of quintuple mutant (NHis-Thal-RebH5)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P13 (MX1) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-06-18 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9763 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.000, 119.110, 87.330 |
Unit cell angles | 90.00, 104.83, 90.00 |
Refinement procedure
Resolution | 49.280 - 1.840 |
R-factor | 0.168 |
Rwork | 0.166 |
R-free | 0.19920 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6h43 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.655 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (dev_3965) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.890 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmeas | 0.077 | 1.182 |
Number of reflections | 95688 | 7071 |
<I/σ(I)> | 14.44 | 1.97 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 6.87 | 6.97 |
CC(1/2) | 0.999 | 0.801 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | reservoir solution: 0.1 M Bicine pH 9.0, 10 % (w/v) PEG 4000, 5 mM tryptophan; protein buffer solution: 10 mM TRIS, 50 mM NaCl, 1 mM TCEP; protein concentration: ~15 mg/mL; drop ratio: 100 nL+100 nL (protein + reservoir) |