1O7D
The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 117.880, 117.880, 582.040 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.700 |
R-factor | 0.257 |
Rwork | 0.257 |
R-free | 0.28900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hty |
RMSD bond length | 0.010 |
RMSD bond angle | 24.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.760 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.090 | 0.540 |
Number of reflections | 60071 | |
<I/σ(I)> | 15.9 | 2.1 |
Completeness [%] | 89.4 * | 77.7 * |
Redundancy | 3 | 3.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | PROTEIN 9 MG/ML IN 20 MM TRIS-CL, PH 7.5, 150 MM NACL MIXED 1:1 WITH 100 MM TRIS-CL, PH 7.5, 50 % SAT. (NH4)2SO4 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 9 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | reservoir | ammonium sulfate | 50 (%sat) | |
5 | 1 | reservoir | Tris-HCl | 100 (mM) | pH7.5 |