5AG3
Chorismatase mechanisms reveal fundamentally different types of reaction in a single conserved protein fold
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-09-12 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 32 |
Unit cell lengths | 116.175, 116.175, 70.429 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 44.812 - 1.898 |
R-factor | 0.1562 |
Rwork | 0.149 |
R-free | 0.18450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4bps |
RMSD bond length | 0.009 |
RMSD bond angle | 1.328 |
Data reduction software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.080 | |
Number of reflections | 83807 | |
<I/σ(I)> | 12.5 | 0.88 |
Completeness [%] | 99.8 | 98.1 |
Redundancy | 5 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | HYG5 WAS CONCENTRATED TO 2.5 TO 3 MG/ML AND AFTERWARDS SUPPLEMENTED WITH 15 MM 3-2-CARBOXYETHYL-BENZOATE EQUILIBRATION AGAINST A RESERVOIR SOLUTION OF 0.1 M MES PH 6.5, 0.2 M AMMONIUM SULFATE AND 20 TO 25 PERCENT PEG 5000 MME |