7KM0

Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59A 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	ROTATING ANODE
Source details	BRUKER X8 PROTEUM
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-02-09
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	1.5418
Spacegroup name	C 2 2 21
Unit cell lengths	84.896, 230.396, 201.723
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	21.300 - 2.600
R-factor	0.2377
Rwork	0.235
R-free	0.29300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ly8
Data reduction software	PROTEUM PLUS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	21.300	2.693
High resolution limit [Å]	2.600	2.600
Rmerge		2.027
Number of reflections	61037	6010
<I/σ(I)>	18.5
Completeness [%]	94.0
Redundancy	15
CC(1/2)	0.990

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	7.4	288.15	0.9 M Magnesium acetate, 8 % PEG 8000, 0.1 M Sodium acetate (pH 7.4), 120 mM R,R-bisLysine