5TX4
Derivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V single amino acid substitutions, bound to human TGF-beta type II receptor ectodomain residues 15-130
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 | 2016-04-02 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 39.019, 70.772, 77.116 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.386 - 1.876 |
| R-factor | 0.195 |
| Rwork | 0.194 |
| R-free | 0.22220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1m9z 5tx2 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.086 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 35.390 |
| High resolution limit [Å] | 1.876 |
| Number of reflections | 17715 |
| <I/σ(I)> | 15.17 |
| Completeness [%] | 99.6 |
| Redundancy | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.1 M Hepes, pH 7.5, 60 % v/v (+/-)-2-Methyl-2,4-pentanediol |






