3H9D
Crystal Structure of Trypanosoma brucei ATG8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Collection date | 2008-09-28 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.100, 48.600, 127.920 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.23773 |
| Rwork | 0.234 |
| R-free | 0.30959 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.414 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 25.000 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 13511 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289 | 3 uL of the protein solution (8 mg ml-1 protein in 100 mM Tris/HCl buffer, pH 6.5) with 3 uL of precipitating solution (22% v/v PEG 4000, 200 mM ammonia sulfate, 100 mM MES, pH 6.5). Droplets were equilibrated against 500 uL of precipitating solution, VAPOR DIFFUSION, HANGING DROP, temperature 289K |






