1GZW
X-RAY CRYSTAL STRUCTURE OF HUMAN GALECTIN-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X31 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-03-15 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.979, 88.805, 93.944 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.410 - 1.700 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.22800 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1slt |
RMSD bond length | 0.005 |
RMSD bond angle | 26.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.410 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.049 | 0.337 |
Total number of observations | 209342 * | |
Number of reflections | 34966 | |
<I/σ(I)> | 12.2 | 5.8 |
Completeness [%] | 96.1 | 91.4 |
Redundancy | 3.9 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 * | CRYSTALS WERE OBTAINED IN SITTING DROPS BY MIXING EQUAL VOLUMES OF THE PROTEIN SOLUTION (10 MG/ML) AND THE PRECIPITATING BUFFER (2M AMMONIUM SULPHATE AND 1% BETA-MERCAPTO ETHANOL, PH 5.0) |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 2 (M) | |
2 | 1 | reservoir | beta-mercaptoethanol | 1 (%) | pH5.6 |
3 | 1 | drop | sodium potassium phosphate | 20 (mM) | |
4 | 1 | drop | lactose | 5 (mM) | pH7.0 |
5 | 1 | drop | protein | 10 (mg/ml) |