1H8O
Three-dimensional structure of anti-ampicillin single chain Fv fragment.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.690, 89.850, 97.260 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 11.940 - 2.750 |
R-factor | 0.178 |
Rwork | 0.178 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 26.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 12.000 | 2.800 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.110 * | 0.400 * |
Total number of observations | 81293 * | |
Number of reflections | 14189 | |
<I/σ(I)> | 8 | 2 |
Completeness [%] | 98.8 | 90.7 |
Redundancy | 3.5 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5 | 20 * | pH 5.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3 (mg/ml) | |
2 | 1 | reservoir | PEG2000 MME | 26 (%(w/v)) | |
3 | 1 | reservoir | ammonium sulfate | 200 (mM) | |
4 | 1 | reservoir | sodium acetate | 100 (mM) | pH5.0 |