3MTF
Crystal structure of the ACVR1 kinase in complex with a 2-aminopyridine inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9762 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 83.688, 138.255, 59.934 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.850 - 2.150 |
| R-factor | 0.18523 |
| Rwork | 0.182 |
| R-free | 0.24421 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h9r |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.603 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.850 | 2.270 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.155 | 0.638 |
| Number of reflections | 35528 | |
| <I/σ(I)> | 10.5 | 2.9 |
| Completeness [%] | 97.3 | 90.5 |
| Redundancy | 7.9 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293.15 | 1.6M Na/KPO4, 0.1M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |
