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2BFV

MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1995-04
DetectorRIGAKU
Spacegroup nameP 32
Unit cell lengths53.600, 53.600, 83.800
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution10.000 - 2.500
R-factor0.176

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Rwork0.187
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1nbv
RMSD bond length0.011
RMSD bond angle0.037
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((ROTAVATA))
Phasing softwareAMoRE
Refinement softwarePROLSQ
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.590
High resolution limit [Å]2.5002.500
Rmerge0.064

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0.225

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Total number of observations12233

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Number of reflections7836
<I/σ(I)>7.212.6
Completeness [%]86.987.5
Redundancy1.51.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.5PROTEIN WAS CRYSTALLIZED FROM 15% (W/V) PEG 4000, 100MM NA ACETATE AND 50MM TRIS HCL PH 8.5
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein2.5-3 (mg/ml)
21dropNa acetate0.05 (M)
31dropTris-HCl0.025 (M)
41dropPEG40007.5 (%(w/v))
51reservoirNa acetate0.1 (M)
61reservoirTris-HCl0.05 (M)
71reservoirPEG400015 (%(w/v))

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PDB entries from 2024-05-01

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