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