6NVA

Crystal structure of Escherichia coli dihydrodipicolinate synthase and propionate covalently bound to K161.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-08-15
Detector	DECTRIS PILATUS 200K
Wavelength(s)	1.54
Spacegroup name	P 1
Unit cell lengths	86.140, 86.333, 107.002
Unit cell angles	109.72, 104.24, 99.18

Refinement procedure

Resolution	25.173 - 2.160
R-factor	0.184
Rwork	0.183
R-free	0.23880
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5t26
RMSD bond length	0.008
RMSD bond angle	0.933
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((1.14_3260: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.200
High resolution limit [Å]	2.160	2.160
Rmerge	0.149	0.756
Number of reflections	142605	6709
<I/σ(I)>	7.781
Completeness [%]	97.6	92
Redundancy	3.2	2
CC(1/2)	0.524	0.524

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	20% PEG 3350 8 mM spermidine 200 mM sodium tartrate 8 mM 2-bromopropionic acid pH 7.5