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2H1J

3.1 A X-ray structure of putative Oligoendopeptidase F: Crystals grown by microfluidic seeding

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 23-ID-D
Synchrotron siteAPS
Beamline23-ID-D
Temperature [K]100
Detector technologyCCD
Collection date2006-04-01
DetectorMARMOSAIC 300 mm CCD
Spacegroup nameP 31 2 1
Unit cell lengths119.324, 119.324, 248.736
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 3.100
R-factor0.18923
Rwork0.187
R-free0.22529
Structure solution methodSAD
RMSD bond length0.011
RMSD bond angle1.131
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareSOLVE
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0003.210
High resolution limit [Å]3.1003.100
Rmerge0.0970.392
Number of reflections37927
<I/σ(I)>9.281.88
Completeness [%]99.9100
Redundancy3.43.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
17296PRECIPITATION FROM A HANGING DROP VAPOR DIFFUSION TRIAL (60% TASCIMATE IN BIS-TRIS PROPANE PH= 7.0) WAS USED TO SEED INTO A 45% TASCIMATE SOLUTION USING A MICROFLUIDIC MICROBATCH SEEDING TECHNIQUE. CONCENTRATION OF PROTEIN WAS 17 MG/ML., TEMPERATURE 296K , pH 7.00

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