3LEG
Lectin Domain of Lectinolysin complexed with Lewis Y Antigen
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2008-05-06 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 67.060, 67.060, 98.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 55.460 - 2.010 |
R-factor | 0.19536 |
Rwork | 0.193 |
R-free | 0.23412 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3leo |
RMSD bond length | 0.018 |
RMSD bond angle | 1.604 |
Data reduction software | d*TREK |
Data scaling software | d*TREK (9.4SSI) |
Phasing software | PHASER (1.3.2) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 55.460 | 67.060 | 2.080 |
High resolution limit [Å] | 2.010 | 4.330 | 2.010 |
Rmerge | 0.143 | 0.064 | 0.492 |
Number of reflections | 15622 | ||
<I/σ(I)> | 9.7 | 21 | 4.1 |
Completeness [%] | 99.8 | 99.1 | 100 |
Redundancy | 11.79 | 10.83 | 11.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 294 | 2M MgSO4, 100mM Tris, pH 8.5, vapor diffusion, hanging drop, temperature 294K |