5FAY
Y208F mutant of choline TMA-lyase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-11-22 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9795 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 228.941, 228.941, 78.952 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.480 - 1.901 |
R-factor | 0.16 |
Rwork | 0.159 |
R-free | 0.19330 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5fau |
RMSD bond length | 0.006 |
RMSD bond angle | 0.925 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 163497 | |
<I/σ(I)> | 12 | 2 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 7.2 | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 294 | Protein at 8 mg/mL in buffer containing 50 mM potassium phosphate pH 8.0, 50 mM potassium chloride, and 10 mM choline was mixed in a 1:1 ratio with well solution containing 1.0-1.2 M sodium malonate pH 7.0-8.0. |