3EO0
Structure of the Transforming Growth Factor-Beta Neutralizing Antibody GC-1008
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2006-02-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97640 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 91.561, 83.009, 91.824 |
| Unit cell angles | 90.00, 103.38, 90.00 |
Refinement procedure
| Resolution | 35.940 - 1.750 |
| R-factor | 0.183 |
| Rwork | 0.182 |
| R-free | 0.20100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v7n |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.524 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.074 | 0.059 | 0.306 |
| Number of reflections | 130926 | ||
| <I/σ(I)> | 12.7 | ||
| Completeness [%] | 97.5 | 95.7 | 85.8 |
| Redundancy | 3.1 | 3 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 20% PEG4000, 0.1M MOPS, pH7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
