6CMZ

2.3 Angstrom Resolution Crystal Structure of Dihydrolipoamide Dehydrogenase from Burkholderia cenocepacia in Complex with FAD and NAD

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2018-02-06
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	83.565, 107.246, 105.427
Unit cell angles	90.00, 106.09, 90.00

Refinement procedure

Resolution	29.210 - 2.300
R-factor	0.20144
Rwork	0.199
R-free	0.25320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lvl
RMSD bond length	0.008
RMSD bond angle	1.466
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MoRDa
Refinement software	REFMAC (5.8.0189)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.109	0.791
Rmeas	0.124	0.909
Rpim	0.059	0.443
Number of reflections	79190	3954
<I/σ(I)>	13.2	1.9
Completeness [%]	100.0	100
Redundancy	4.4	4.1
CC(1/2)		0.624

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	295	Protein: 8.0 mg/ml, 0.5 Sodium chloride, 0.01M Tris pH 8.3, 1mM FAD; Screen: PACT (D1), 0.1M MMT buffer pH 4.0, 25% (w/v) PEG 1500