1P2C
crystal structure analysis of an anti-lysozyme antibody
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-02-10 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 44.660, 73.750, 83.780 |
Unit cell angles | 66.59, 74.74, 85.44 |
Refinement procedure
Resolution | 20.000 - 2.000 |
Rwork | 0.204 |
R-free | 0.24200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | D44.1 Fab |
RMSD bond length | 0.006 * |
RMSD bond angle | 1.395 * |
Data reduction software | CrystalClear ((MSC/RIGAKU)) |
Data scaling software | CrystalClear ((MSC/RIGAKU)) |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 2.000 | 2.070 |
High resolution limit [Å] | 2.000 * | 2.000 |
Rmerge | 0.013 | 0.036 |
Number of reflections | 60488 | |
Completeness [%] | 95.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 298 | PEG 1000, CaCl2, pH 4.6, vapor diffusion, temperature 298.K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris | 5 (mM) | pH7.5 |
3 | 1 | reservoir | PEG1000 | 28 (%) | |
4 | 1 | reservoir | 0.2 (M) | pH4.6 |