4K3I

Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG, C2 Space Group

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2010-04-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.03320
Spacegroup name	C 1 2 1
Unit cell lengths	346.356, 55.558, 112.548
Unit cell angles	90.00, 106.55, 90.00

Refinement procedure

Resolution	43.060 - 2.000
R-factor	0.14602
Rwork	0.144
R-free	0.19013
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3sxt
RMSD bond length	0.020
RMSD bond angle	2.065
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.030
High resolution limit [Å]	2.000	2.000
Number of reflections	132241
<I/σ(I)>	13.55	2.65
Completeness [%]	99.8	99.5
Redundancy	4.8	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.4	293	Drops contained 1uL protein with 3uL reservoir solution. WT-MauG and MADH were each reduced in an anaerobic glove box prior to preparing the protein mixture for crystallization. Protein mixture: 100uM reduced WT-MauG and 50uM reduced MADH in 10mM potassium phosphate pH7.5 with 2mM sodium dithionite. Reservoir solution contained: 24% w/v PEG 8000, 0.1M sodium acetate, 0.1M MES pH 6.4 and 2mM sodium dithionite. Crystallization was carried out in an anaerobic glove box at ambient temperature., VAPOR DIFFUSION, HANGING DROP, temperature 293K