5F3B
Structure of myostatin in complex with chimeric RK35 antibody
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2010-08-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 66.090, 67.616, 78.559 |
| Unit cell angles | 78.98, 88.77, 67.44 |
Refinement procedure
| Resolution | 49.170 - 1.760 |
| R-factor | 0.1807 |
| Rwork | 0.179 |
| R-free | 0.20570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gcy |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 100.000 |
| High resolution limit [Å] | 1.760 |
| Number of reflections | 104791 |
| Redundancy | 1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | Chimeric RK35 Fab and myostatin were purified and the protein complex was concentrated to 10.75 mg/ml in a buffer of 50 mM tris hydrochloride pH 7.5 and 100 mM sodium chloride. Crystals were obtained using the hanging drop method with equilibration at 18C against a solution containing 20% PEG MME 5000 and 100 mM bis-tris pH 6.5 |






