1W6Q
X-RAY CRYSTAL STRUCTURE OF R111H HUMAN GALECTIN-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.130, 58.180, 111.780 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.650 - 2.100 |
R-factor | 0.242 |
Rwork | 0.242 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gzw |
RMSD bond length | 0.010 |
RMSD bond angle | 1.400 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.050 | 0.240 |
Number of reflections | 16802 | |
<I/σ(I)> | 9.2 | 4.4 |
Completeness [%] | 97.6 | 94.6 |
Redundancy | 3.9 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | CRYSTALS WERE OBTAINED IN SITTING DROPS BY MIXING EQUAL VOLUMES OF THE PROTEIN SOLUTION (10 MG/ML) AND THE PRECIPITATING BUFFER (30% (V/V) PEG4000, 1% BETA-MERCAPTO ETHANOL AND N-BUTANOL, PH 5.6) |