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2O9O

Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution

Replaces:  1SV8
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]278
Detector technologyIMAGE PLATE
Collection date2003-12-10
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 21 21 21
Unit cell lengths63.100, 66.859, 108.543
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.800
R-factor0.18843
Rwork0.186
R-free0.23619
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2esc
RMSD bond length0.019
RMSD bond angle1.865
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.850
High resolution limit [Å]2.8002.800
Number of reflections11349
<I/σ(I)>112.7
Completeness [%]97.195.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.8298TRIS-HCL, NACL, 19% ETHANOL, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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