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3G2M

Crystal Structure of the Glycopeptide N-methyltransferase MtfA

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X8C
Synchrotron siteNSLS
BeamlineX8C
Temperature [K]100
Detector technologyCCD
Collection date2007-02-17
Wavelength(s)0.9800
Spacegroup nameC 1 2 1
Unit cell lengths127.443, 71.682, 75.189
Unit cell angles90.00, 103.02, 90.00
Refinement procedure
Resolution50.000 - 2.000
R-factor0.239
Rwork0.238
R-free0.27100
Structure solution methodSAD
RMSD bond length0.007
RMSD bond angle1.054
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHELXS
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]50.00050.0002.070
High resolution limit [Å]2.0004.3102.000
Rmerge0.0460.0370.315
Number of reflections45124
<I/σ(I)>20.585
Completeness [%]97.499.184.6
Redundancy2.52.62.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.52940.1M MES pH 6.5, 18% PEG-monomethyl ether 5K, vapor diffusion, hanging drop, temperature 294K

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