8GEK

Dihydrodipicolinate synthase with pyruvate from Candidatus Liberibacter solanacearum

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	110
Detector technology	CCD
Collection date	2018-12-01
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9537
Spacegroup name	C 1 2 1
Unit cell lengths	101.112, 132.920, 154.904
Unit cell angles	90.00, 99.79, 90.00

Refinement procedure

Resolution	45.810 - 1.930
R-factor	0.1864
Rwork	0.185
R-free	0.22470
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.968
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.810	1.960
High resolution limit [Å]	1.930	1.930
Rmerge	0.082
Number of reflections	151510	6831
<I/σ(I)>	7.8
Completeness [%]	99.5
Redundancy	3.94
CC(1/2)	0.998	0.468

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Crystallization trials used the sitting drop vapour diffusion method, at 20 C, with droplets consisting of 150 nL of protein solution and 150 nL of reservoir solution. Rectangular CLsoDHDPS crystals were produced using the JCSG+ Suite screen in condition A2 (20% w/v polyethylene glycol 3000, 0.1 M sodium citrate, pH 5.5). For ligand bound structures, the crystals were soaked for 7 days in mother liquor with either: 100 mM lysine, 100 mM pyruvate or 100 mM of both succinic semi-aldehyde and pyruvate.