3LXC
Interconversion of Human Lysosomal Enzyme Specificities
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-15 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.07188 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 89.947, 139.492, 182.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.690 - 2.350 |
R-factor | 0.186 |
Rwork | 0.184 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hg3 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.172 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.390 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.153 | 0.862 |
Number of reflections | 47535 | |
<I/σ(I)> | 12.3 | 2 |
Completeness [%] | 98.6 | 98.7 |
Redundancy | 4.1 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG8000, Sodium Cacodylate, Magnesium Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |