1E4W
crossreactive binding of a circularized peptide to an anti-TGFalpha antibody Fab-fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-06-17 |
| Detector | XRAY RESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.220, 94.350, 121.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.950 |
| R-factor | 0.204 * |
| Rwork | 0.204 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fbi |
| RMSD bond length | 0.016 * |
| RMSD bond angle | 0.045 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.500 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.081 | 0.288 |
| Number of reflections | 39968 | |
| <I/σ(I)> | 19.5 | 5.7 |
| Completeness [%] | 94.6 | 54.2 |
| Redundancy | 9.9 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 | PROTEIN IN TRIS-HCL, 8.5 11-14 MG/ML PRECIPITANT: 12% PEG MME 2000, 5 MM NICL2, 0.1 M TRIS-HCL, PH 8.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG2000 MME | 12 (%) | |
| 2 | 1 | reservoir | 5 (mM) | ||
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
| 4 | 1 | drop | protein | 11-14 (mg/ml) | |
| 5 | 1 | drop | Tris-HCl | 20 (mM) | pH8.5 |
