1HCF
Crystal structure of TrkB-d5 bound to neurotrophin-4/5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX14.1 |
| Synchrotron site | SRS |
| Beamline | PX14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-03-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 74.372, 80.406, 91.318 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.700 |
| R-factor | 0.218 |
| Rwork | 0.218 |
| R-free | 0.26400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1B98 (NEUROTROPHIN) 1WWB (TRK) |
| RMSD bond length | 0.007 |
| RMSD bond angle | 26.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.084 * | 0.294 * |
| Number of reflections | 15635 | |
| <I/σ(I)> | 19.6 | 3.7 |
| Completeness [%] | 99.2 | 99.9 |
| Redundancy | 5.4 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 | 10 MG/ML COMPLEX IN 20MM TRIS, 150MM NACL, PH 7.5, 100MM HEPES PH 7.5, 1.5M LISO4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 10 (mg/ml) | |
| 2 | 1 | 2 | 1.5-1.6 (M) | ||
| 3 | 1 | 2 | HEPES | 100 (mM) | pH7.0-7.5 |






