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2AAK

UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA

Replaces:  1AAK
Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]295
Detector technologyAREA DETECTOR
Collection date1992-01
DetectorSIEMENS
Spacegroup nameP 21 21 21
Unit cell lengths41.800, 44.900, 83.200
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution100.000 - 2.400
R-factor0.221
Rwork0.221
R-free0.28700
Structure solution methodMULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length0.009
RMSD bond angle24.800

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Data reduction softwareXENGEN
Data scaling softwareXENGEN
Phasing softwareX-PLOR (3.851)
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 Overall
Low resolution limit [Å]100.000
High resolution limit [Å]2.400
Rmerge0.077

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Total number of observations40453

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Number of reflections6377
Completeness [%]97.9
Redundancy6.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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6.7Cook, W.J., (1992) J.Mol.Biol., 223, 1183.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21dropammonium sulfate17.5 (%(w/v)sat)
31dropMES0.025 (M)
41reservoirammonium sulfate35 (%sat)
51reservoirMES0.05 (M)

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