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1AA0

FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]298
Detector technologyIMAGE PLATE
Collection date1995-07-01
DetectorRIGAKU RAXIS IIC
Spacegroup nameH 3 2
Unit cell lengths41.200, 41.200, 358.700
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.200
R-factor0.216
Rwork0.216
R-free0.26700

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Structure solution methodMIR
RMSD bond length0.010

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RMSD bond angle1.300

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.240
High resolution limit [Å]2.2002.200
Rmerge0.053

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Total number of observations57901

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Number of reflections6490

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<I/σ(I)>152
Completeness [%]92.656.6
Redundancy4.82.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5

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22

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PROTEIN WAS CRYSTALLIZED AT 22OC USING 34% PEG400, 0.1M ZN ACETATE IN 0.1M MES BUFFER AT PH6.0 AS WELL SOLUTION BY MIXING EQUAL AMOUNT OF WELL SOLUTION AND PROTEIN SOLUTION AT 29MG/ML IN A HANGING DROP, vapor diffusion - hanging drop
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein29 (mg/ml)
21dropTris-HCl10 (mM)pH7.5
31reservoirPEG40034 (%)
41reservoirzinc acetate0.1 (M)
51reservoirMES0.1 (M)pH6.0

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