5TS9
Crystal structure of Chorismate mutase from Burkholderia phymatum
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 | 2016-10-12 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.590, 151.120, 73.080 |
Unit cell angles | 90.00, 90.84, 90.00 |
Refinement procedure
Resolution | 47.879 - 1.950 |
R-factor | 0.1566 |
Rwork | 0.156 |
R-free | 0.20590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4oj7 chain A |
RMSD bond length | 0.009 |
RMSD bond angle | 0.923 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.000 | |
High resolution limit [Å] | 1.950 | 8.720 | 1.950 |
Rmerge | 0.094 | 0.039 | 0.519 |
Number of reflections | 98259 | ||
<I/σ(I)> | 11.7 | 28.91 | 3.01 |
Completeness [%] | 99.7 | 98.3 | 99.7 |
Redundancy | 4.25 | ||
CC(1/2) | 0.996 | 0.997 | 0.808 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.6 | 290 | Microlytic MCSG 1 screen D5: 200mM Ammonium formate pH 6.6, 20% PEG 3350; BuphA.00160.b.B2.PS37873 at 22.4mg/ml; cryo: 10% EG; tray 272085d5, puck LQB7-3 |