1B98
NEUROTROPHIN 4 (HOMODIMER)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL1-5 |
| Synchrotron site | SSRL |
| Beamline | BL1-5 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.800, 50.800, 53.000 |
| Unit cell angles | 90.00, 109.40, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.350 * |
| R-factor | 0.235 |
| Rwork | 0.235 |
| R-free | 0.33600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NT4 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.048 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.350 * |
| Rmerge | 0.031 |
| Number of reflections | 7858 |
| Completeness [%] | 93.0 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 * | 15 * | PEG 8000, PIPES, pH 6.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | reservoir | PEG8000 | 22 (%) | |
| 4 | 1 | reservoir | PIPES | 100 (mM) | |
| 5 | 1 | drop | 24 amino acid peptide | 1:2 ratio (NT4 protomer:peptide) |






