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1PJ6

Crystal structure of dimethylglycine oxidase of Arthrobacter globiformis in complex with folic acid

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineX11
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2002-05-01
DetectorMARRESEARCH
Wavelength(s)0.9
Spacegroup nameC 2 2 2
Unit cell lengths70.877, 222.506, 119.304
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000

*

- 1.650
R-factor0.15752
Rwork0.156
R-free0.19300

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1pj5
RMSD bond length0.016
RMSD bond angle1.634
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.1.08)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0001.700
High resolution limit [Å]1.6501.650
Rmerge0.0670.346

*

Number of reflections106504
<I/σ(I)>11.9
Completeness [%]99.399
Redundancy5.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.529415% PEG 2000MME, 0.2 MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21reservoirPEG5000 MME15 (%)
31reservoir0.2 (M)pH7.5
41reservoirHEPES0.1 (M)

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