3FBX
Crystal structure of the lysosomal 66.3 kDa protein from mouse solved by S-SAD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-05-06 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.9000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 148.804, 89.672, 64.954 |
| Unit cell angles | 90.00, 98.67, 90.00 |
Refinement procedure
| Resolution | 32.110 - 2.400 |
| R-factor | 0.15817 |
| Rwork | 0.156 |
| R-free | 0.19804 |
| Structure solution method | SAD |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.436 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.083 | 0.373 |
| Number of reflections | 32641 | |
| <I/σ(I)> | 48.813 | 10.2 |
| Completeness [%] | 98.9 | 97.5 |
| Redundancy | 23 | 21.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | 12% (w/v) PEG 4000, 200mM NH4Ac, 100mM NaAc/HAc pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
