7AQU
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 | 54.580, 118.570, 87.100 |
Unit cell angles | 90.00, 104.04, 90.00 |
Refinement procedure
Resolution | 48.579 - 1.630 |
Rwork | 0.167 |
R-free | 0.20230 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6H43 chain A |
RMSD bond length | 0.010 |
RMSD bond angle | 1.595 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.670 |
High resolution limit [Å] | 1.630 | 1.630 |
Rmeas | 0.079 | 1.146 |
Number of reflections | 129082 | 8424 |
<I/σ(I)> | 15.33 | 1.97 |
Completeness [%] | 96.6 | 85.3 |
Redundancy | 7.03 | 6.73 |
CC(1/2) | 0.999 | 0.748 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293.5 | reservoir solution: 0.1 M bicine pH 9.0, 20 % (w/v) PEG 4000, 10 % (v/v) glycerol, 0.02 M amino acid mix consisting of L-Glu, L-Ala, D-Ala, Gly, L-Lys, D-Lysis, L-Ser and D-Ser; 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) |