5F3H
Structure of myostatin in complex with humanized 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] | 100 |
Detector technology | CCD |
Collection date | 2010-10-18 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 |
Unit cell lengths | 75.138, 80.916, 101.401 |
Unit cell angles | 88.33, 103.78, 92.40 |
Refinement procedure
Resolution | 19.990 - 2.700 |
R-factor | 0.2208 |
Rwork | 0.218 |
R-free | 0.26990 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5f3b |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | PHENIX |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.700 |
Number of reflections | 40287 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | Humanized RK35 Fab and myostatin were purified and the protein complex was concentrated to 10 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 an unbuffered solution containing 20% PEG 3350 and 200mM sodium chloride. |