8SC0

Crystal Structure of 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase from Klebsiella aerogenes (NAD bound, orthorhombic form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-02-14
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9795
Spacegroup name	P 21 21 21
Unit cell lengths	71.970, 91.942, 144.165
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.590 - 1.810
R-factor	0.1711
Rwork	0.169
R-free	0.20510
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.637
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.21rc1_4918: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	91.940	1.850
High resolution limit [Å]	1.800	1.800
Rmerge	0.122	1.419
Rmeas	0.127	1.478
Rpim	0.035	0.412
Total number of observations	1145982	82195
Number of reflections	89308	6485
<I/σ(I)>	13	2
Completeness [%]	100.0
Redundancy	12.8	12.7
CC(1/2)	0.998	0.765

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.4	291	JCSG+ D12: 0.04 M Pottasium Phosphate, 16% PEG 8K, 20% Glycerol. KlaeA.01365.a.B1.PW39175 at 21.8 mg/mL. 2mM NAD added to the protein prior to crystallization. Plate: 13164, well D12 drop 2, Puck: PSL-0615, Cryo: Direct. Subunits C and D contain NAD. Subunits A and B have interlaced alternate conformations from residues 180-196 and were refined with partial occupancies