1KRF
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 | 2000-03-20 |
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 | 0.199 * |
Rwork | 0.199 |
R-free | 0.23640 |
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 | 2.200 |
High resolution limit [Å] | 2.140 | 2.140 |
Rmerge | 0.074 | 0.376 * |
Total number of observations | 225764 * | |
Number of reflections | 57692 | |
<I/σ(I)> | 20.1 | |
Completeness [%] | 98.7 | 89.3 |
Redundancy | 3.91 |
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 |