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3ZC9

Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 4.6

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsBRUKER
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2011-01-22
DetectorMAR scanner 345 mm plate
Spacegroup nameC 1 2 1
Unit cell lengths101.620, 45.420, 38.790
Unit cell angles90.00, 94.87, 90.00
Refinement procedure
Resolution50.630 - 2.240
R-factor0.19352
Rwork0.191
R-free0.23798
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3iir
RMSD bond length0.006
RMSD bond angle1.235
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.6302.330
High resolution limit [Å]2.2102.210
Rmerge0.0700.220
Number of reflections7985
<I/σ(I)>13.75.7
Completeness [%]90.060.3
Redundancy3.53.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
14.64M AMMONIUM ACETATE, 0.1M SODIUM ACETATE TRIHYDRATE PH 4.6

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