3ETV
Crystal structure of a Tip20p-Dsl1p fusion protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0400 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 168.430, 61.358, 37.277 |
| Unit cell angles | 90.00, 91.96, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.940 |
| R-factor | 0.22737 |
| Rwork | 0.225 |
| R-free | 0.27722 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3etu |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.091 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.020 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Number of reflections | 25475 | |
| <I/σ(I)> | 18 | 2 |
| Completeness [%] | 90.7 | 97 |
| Redundancy | 3.1 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5 | 298 | 5:5:1 ratio of protein, well buffer (0.1 M sodium acetate, pH 5.0, 0.2 M ammonium acetate, 20% (w/v) PEG 4000), and additive (1.0 M lithium chloride) , VAPOR DIFFUSION, temperature 298.0K |
