1KWU
Rat mannose binding protein A complexed with a-Me-Man
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-08-26 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 78.890, 85.370, 98.270 |
Unit cell angles | 90.00, 106.30, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.950 |
Rwork | 0.207 |
R-free | 0.24100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.010 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.039 * | 0.257 |
Number of reflections | 43124 | |
Completeness [%] | 94.1 | 88.9 |
Redundancy | 1.9 * | 1.8 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 20-22 * | 8-13% PEG 8000 or 3500, 100mM Tris-Cl pH=8.0, 10mM NaCl, 20mM Cacl2, 2mM NaN3. Protein solution: 12mg/ml in 10 mM NaCl, 10mM CaCl2. VAPOR DIFFUSION, HANGING DROP at 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | drop | 10 (mM) | ||
3 | 1 | reservoir | PEG3350 | 8-13 (%) | or PEG8000 |
4 | 1 | reservoir | Tris-Cl | 100 (mM) | pH8.0 |
5 | 1 | reservoir | 10 (mM) | ||
6 | 1 | reservoir | 20 (mM) | ||
7 | 1 | reservoir | 2 (mM) |