6MLX
Crystal structure of T. pallidum Leucine Rich Repeat protein (TpLRR)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL14-1 |
| Synchrotron site | SSRL |
| Beamline | BL14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-03-05 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.9202 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 104.079, 104.079, 185.808 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 69.308 - 2.000 |
| R-factor | 0.2366 |
| Rwork | 0.234 |
| R-free | 0.28150 |
| Structure solution method | SAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.927 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 92.900 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 67107 | |
| <I/σ(I)> | 15.1 | |
| Completeness [%] | 96.2 | |
| Redundancy | 9.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 0.1 M Bis-Tris HCl, pH 6.5 and 25% PEG 3350 |






