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1A78

COMPLEX OF TOAD OVARY GALECTIN WITH THIO-DIGALACTOSE

Experimental procedure
Source typeROTATING ANODE
Source detailsRIGAKU RUH3R
Temperature [K]300
Detector technologyIMAGE PLATE
Collection date1994-12
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 1 21 1
Unit cell lengths51.800, 51.000, 56.300
Unit cell angles90.00, 97.20, 90.00
Refinement procedure
Resolution6.000 - 2.000
R-factor0.194
Rwork0.194
R-free0.25600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gan
RMSD bond length0.011
RMSD bond angle28.120

*

Data reduction softwareR-AXIS (V. 3.4)
Data scaling softwareR-AXIS (V 3.4)
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 Overall
Low resolution limit [Å]15.000
High resolution limit [Å]1.945
Rmerge0.086
Total number of observations32134

*

Number of reflections14540
Completeness [%]68.6
Redundancy2.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

6.6DROPS OF EQUAL AMOUNT OF 10-12 MG/ML PROTEIN AND RESERVOIR SOLUTION WERE EQUILIBRATED AGAINST 1 ML OF (NH4)2SO4 AT 56% SATURATION IN 100MM TRIS-ACETATE BUFFER, PH 6.6 AND 1% MPD AND 1% DTT
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10-12 (mg/ml)
21reservoirammonium sulfate56 (%sat)
31reservoirTris-acetate100 (mM)pH6.6
41reservoirMPD1 (%)
51reservoirdithiothreitol1 (mM)

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