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3SXT

Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-B
Synchrotron siteAPS
Beamline23-ID-B
Temperature [K]100
Detector technologyCCD
Collection date2011-06-29
DetectorMARMOSAIC 300 mm CCD
Spacegroup nameP 1 21 1
Unit cell lengths62.639, 135.664, 111.557
Unit cell angles90.00, 97.37, 90.00
Refinement procedure
Resolution35.010 - 1.810
R-factor0.147
Rwork0.145
R-free0.18700
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3l4m
RMSD bond length0.026
RMSD bond angle2.092
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareREFMAC (5.5.0109)
Refinement softwareREFMAC (5.5.0109)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.840
High resolution limit [Å]1.8101.810
Number of reflections164390
<I/σ(I)>16.72.3
Completeness [%]98.380.9
Redundancy6.52.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
16.4293Drops 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: 22% 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

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