1DEX
RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 291 |
Detector technology | IMAGE PLATE |
Collection date | 1996-07-19 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.550, 57.080, 71.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.162 * |
Rwork | 0.162 |
R-free | 0.21800 |
RMSD bond length | 0.014 |
RMSD bond angle | 24.500 * |
Data reduction software | ROTAVATA |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | MLPHARE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.062 | 0.258 |
Number of reflections | 15662 | |
<I/σ(I)> | 9.2 | |
Completeness [%] | 89.7 | 64.1 |
Redundancy | 4.1 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 5 * | 298 | PEG 4000, 2-propanol, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | 1.4 (M) | ||
2 | 1 | 1 | sodium acetate | 0.1 (M) | |
3 | 1 | 1 | protein | 40 (OD280) |