1KTR
Crystal Structure of the Anti-His Tag Antibody 3D5 Single-Chain Fragment (scFv) in Complex with a Oligohistidine peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-10-02 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.873 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 106.510, 106.510, 92.800 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.700 |
| R-factor | 0.1904 * |
| Rwork | 0.190 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | VL: PDB ENTRY 1TET VH: PDB ENTRY 1PSK |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.317 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.116 | 0.537 |
| Total number of observations | 128480 * | |
| Number of reflections | 16996 | |
| <I/σ(I)> | 16.6 | 4.4 |
| Completeness [%] | 99.0 | 99.8 |
| Redundancy | 7.6 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.4 | 4 * | PEG 8000, magnesium acetate, MES, pH 6.4, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 3.8 (mg/ml) | |
| 2 | 1 | reservoir | MES | 0.1 (M) | pH6.4 |
| 3 | 1 | reservoir | magnesium acetate | 0.2 (M) | |
| 4 | 1 | reservoir | PEG8000 | 20 (%(w/v)) | |
| 5 | 1 | reservoir | 0.02 (%(w/v)) |
