2P6A
The structure of the Activin:Follistatin 315 complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 5ID-B |
| Synchrotron site | APS |
| Beamline | 5ID-B |
| Temperature [K] | 298 |
| Detector technology | CCD |
| Collection date | 2006-06-26 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 2 2 21 |
| Unit cell lengths | 104.641, 106.584, 87.568 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.010 - 3.400 |
| R-factor | 0.225 |
| Rwork | 0.223 |
| R-free | 0.32400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | one activin A monomer and ND FSD1 and FSD2 of one follistatin 288 molecule (PDB 2B0U) |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.945 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 34.344 | 40.390 | 3.580 |
| High resolution limit [Å] | 3.400 | 10.750 | 3.400 |
| Rmerge | 0.160 | 0.072 | 0.708 |
| Total number of observations | 2786 | 14619 | |
| Number of reflections | 13978 | ||
| <I/σ(I)> | 4 | 8.8 | 1 |
| Completeness [%] | 99.7 | 92.5 | 100 |
| Redundancy | 7.2 | 6 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 20-23% PEG 1000, 200mM MgCl2, 3% EtOH, 20mM Trimethyl-amine HCl, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298 K |
