5O95
Structure of the putative methyltransferase Lpg2936 from Legionella pneumophila
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 | 2015-02-12 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.9650 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.785, 144.777, 64.086 |
| Unit cell angles | 90.00, 100.13, 90.00 |
Refinement procedure
| Resolution | 47.560 - 1.491 |
| R-factor | 0.1806 |
| Rwork | 0.179 |
| R-free | 0.20950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nxz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.857 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.560 | 1.570 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.044 | 0.752 |
| Number of reflections | 173267 | |
| <I/σ(I)> | 10.6 | 1.1 |
| Completeness [%] | 95.0 | 89.3 |
| Redundancy | 2.4 | 2.3 |
| CC(1/2) | 0.999 | 0.725 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289 | Optimised from morpheus screen: Mes/Imidazole pH 6.5 0.1 M EDO_Peg8K 27% Alcohols: 0.14 M |
