1NXC
Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-D |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-04-22 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.288, 72.164, 129.571 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 62.500 - 1.510 |
| R-factor | 0.17174 |
| Rwork | 0.171 |
| R-free | 0.18970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.382 |
| Data reduction software | PROTEUM PLUS ((BRUKER)) |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.500 | 1.630 |
| High resolution limit [Å] | 1.510 | 1.510 |
| Number of reflections | 73142 | |
| <I/σ(I)> | 10.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | PEG4000, pH 4.5-6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
