1KRE
STRUCTURE OF P. CITRINUM ALPHA 1,2-MANNOSIDASE REVEALS THE BASIS FOR DIFFERENCES IN SPECIFICITY OF THE ER AND GOLGI CLASS I ENZYMES
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | AREA DETECTOR |
| Collection date | 2000-04-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.487, 110.997, 86.235 |
| Unit cell angles | 90.00, 99.17, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.200 |
| R-factor | 0.198 * |
| Rwork | 0.198 |
| R-free | 0.24290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kkt |
| RMSD bond length | 0.006 * |
| RMSD bond angle | 1.200 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.150 |
| High resolution limit [Å] | 2.030 | 2.030 |
| Rmerge | 0.091 | 0.615 * |
| Total number of observations | 226590 * | |
| Number of reflections | 63769 | |
| <I/σ(I)> | 16.8 | |
| Completeness [%] | 93.2 | 73.8 |
| Redundancy | 3.55 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 * | 293 | PEG 6000, potassium phosphate, pH 4.60, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | sodium acetate | 10 (mM) | pH5.0 |
| 3 | 1 | reservoir | PEG6000 | 17-22 (%) | |
| 4 | 1 | reservoir | potassium phosphate | 50 (mM) | pH4.6 |
