1FO3
CRYSTAL STRUCTURE OF HUMAN CLASS I ALPHA1,2-MANNOSIDASE IN COMPLEX WITH KIFUNENSINE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 1999-10-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 95.975, 95.975, 137.028 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.560 - 1.750 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.24100 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.800 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.065 | 0.480 |
Total number of observations | 406202 * | |
Number of reflections | 73653 * | |
<I/σ(I)> | 9.4 | |
Completeness [%] | 99.4 | 100 |
Redundancy | 5.5 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | MES, calcium, kifunensine, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | MES | 20 (mM) | |
3 | 1 | drop | 150 (mM) | ||
4 | 1 | drop | 5 (mM) | ||
5 | 1 | drop | NDSB201 | 0.25 (M) | |
6 | 1 | reservoir | ammonium sulfate | 1.6-1.7 (M) |