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 |
