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3O2E

Crystal structure of a bol-like protein from babesia bovis

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU MICROMAX-007 HF
Temperature [K]100
Detector technologyCCD
Collection date2009-05-20
DetectorRIGAKU SATURN 944
Wavelength(s)1.5418
Spacegroup nameP 41 21 2
Unit cell lengths66.300, 66.300, 35.290
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.530 - 1.950
R-factor0.185
Rwork0.183
R-free0.24100
Structure solution methodSAD
Starting model (for MR)iodide SAD
RMSD bond length0.018
RMSD bond angle1.712
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwarePHASER
Refinement softwareREFMAC (5.5.0109)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.000
High resolution limit [Å]1.9501.950
Rmerge0.0940.481
Number of reflections6133
<I/σ(I)>19.394.4
Completeness [%]99.799.6
Redundancy18.37
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP6.5290EBS JCSG SCREEN E2: 2M AMMONIUM SULPHATE, 100MM CACODYLATE PH 6.5, 200MM NACL: BABOA.10365.A AT 12.4MG/ML, ENCUA.00735 AT 29.3MG/ML, PH N/A, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K

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