7KM1

Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59N mutant with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-10-09
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9795
Spacegroup name	C 2 2 21
Unit cell lengths	85.010, 230.450, 200.640
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.556 - 1.840
R-factor	0.1827
Rwork	0.181
R-free	0.21130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ly8
RMSD bond length	0.005
RMSD bond angle	0.903
Data reduction software	HKL-3000
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (dev_2398)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.556	1.906
High resolution limit [Å]	1.840	1.840
Rmerge		0.544
Number of reflections	167633	16793
<I/σ(I)>	16.24
Completeness [%]	98.6	99.79
Redundancy	15
CC(1/2)	0.990

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	7.4	288.15	0.5 M Magnesium acetate, 8 % PEG 8000, 0.1 M Sodium acetate (pH 7.4), 120 mM R,R-bisLysine