1EA9
Cyclomaltodextrinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 6B |
Synchrotron site | PAL/PLS |
Beamline | 6B |
Temperature [K] | 100 |
Spacegroup name | F 2 3 |
Unit cell lengths | 334.608, 334.608, 334.608 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 3.200 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.25600 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 * |
RMSD bond angle | 1.226 |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | |
High resolution limit [Å] | 3.200 | |
Rmerge | 0.063 | 0.178 * |
Total number of observations | 671314 * | |
Number of reflections | 51030 * | |
<I/σ(I)> | 12.29 | |
Completeness [%] | 90.2 | 85.8 * |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 22 * | pH 7.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
3 | 1 | drop | beta-mercaptoethanol | 1 (mM) | |
4 | 1 | reservoir | PEG200 | 50 (%) | |
5 | 1 | reservoir | HEPES | 0.1 (M) | pH7.0 |