1A78
COMPLEX OF TOAD OVARY GALECTIN WITH THIO-DIGALACTOSE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 300 |
Detector technology | IMAGE PLATE |
Collection date | 1994-12 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.800, 51.000, 56.300 |
Unit cell angles | 90.00, 97.20, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.000 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gan |
RMSD bond length | 0.011 |
RMSD bond angle | 28.120 * |
Data reduction software | R-AXIS (V. 3.4) |
Data scaling software | R-AXIS (V 3.4) |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 15.000 |
High resolution limit [Å] | 1.945 |
Rmerge | 0.086 |
Total number of observations | 32134 * |
Number of reflections | 14540 |
Completeness [%] | 68.6 |
Redundancy | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.6 | DROPS 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
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-12 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 56 (%sat) | |
3 | 1 | reservoir | Tris-acetate | 100 (mM) | pH6.6 |
4 | 1 | reservoir | MPD | 1 (%) | |
5 | 1 | reservoir | dithiothreitol | 1 (mM) |