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2TRY

TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH2R
Temperature [K]296
Detector technologyIMAGE PLATE
Collection date1995-12
DetectorRIGAKU
Spacegroup nameP 21 21 2
Unit cell lengths43.670, 86.370, 64.940
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution5.000 - 2.000
R-factor0.213
Rwork0.213
R-free0.31000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1tta
RMSD bond length0.012
RMSD bond angle1.900
Data reduction softwarebioteX
Data scaling softwarebioteX
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]64.9002.000
High resolution limit [Å]1.8001.800
Rmerge0.1070.270
Number of reflections17581
<I/σ(I)>51.8
Completeness [%]74.956
Redundancy2.21.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
16.5PURIFIED PROTEIN (25MG/ML IN 100MM TRIS BUFFER, PH 7.5) WAS CRYSTALLIZED FROM 1.5M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5, AT ROOM TEMPERATURE., pH 6.5

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