5LVA
Crystal structure of thermophilic tryptophan halogenase (Th-Hal) enzyme from Streptomycin violaceusniger.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 180 |
Detector technology | PIXEL |
Collection date | 2014-11-28 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.979 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 66.840, 66.840, 335.000 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 51.391 - 2.530 |
R-factor | 0.1856 |
Rwork | 0.183 |
R-free | 0.23830 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.185 |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 54.710 |
High resolution limit [Å] | 2.530 |
Number of reflections | 15952 |
<I/σ(I)> | 19.7 |
Completeness [%] | 99.9 |
Redundancy | 18.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.1 M amino acids in a 0.1 M buffer (1.0M imidazole + MES monohydrate acid buffer) at pH 6.5 made up with a 50% v/v precipitant mix (that contained 10% w/v PEG 20,000; 20% v/v PEG MME 550) |