6F5D
Trypanosoma brucei F1-ATPase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-06-19 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.966 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 124.218, 206.350, 130.210 |
| Unit cell angles | 90.00, 104.85, 90.00 |
Refinement procedure
| Resolution | 90.510 - 3.200 |
| R-factor | 0.27297 |
| Rwork | 0.272 |
| R-free | 0.29712 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2jdi |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.066 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER (2.7.17) |
| Refinement software | REFMAC (5.8.0190) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.510 | 3.250 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.123 | 0.565 |
| Number of reflections | 102391 | |
| <I/σ(I)> | 8.1 | |
| Completeness [%] | 98.2 | 97.6 |
| Redundancy | 3.5 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 277 | 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgSO4 and 1 mM ADP, 7.7% (w/v) polyethyleneglycol 10000 dissolved in a buffer containing 100 mM 2-(N-morpholino)-ethanesulfonic acid, pH 6.0 |
