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 |