1MDP
REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN
Experimental procedure
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.510, 88.330, 75.790 |
Unit cell angles | 90.00, 95.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.187 |
Rwork | 0.187 |
RMSD bond length | 0.009 |
RMSD bond angle | 0.025 * |
Phasing software | X-PLOR |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.250 * |
Rmerge | 0.042 * |
Total number of observations | 62502 * |
Number of reflections | 39720 |
Completeness [%] | 74.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 * | microseeding into drops of 18-20 % PEG over 18-25 % PEG * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4 (mg/ml) | |
2 | 1 | drop | maltose | 2-3 (mM) | |
3 | 1 | drop | PEG6000 | 10-12.5 (%) | |
4 | 1 | drop | sodium citrate | 10 (mM) | |
5 | 1 | drop | sodium azide | 0.02 (%) | |
6 | 1 | reservoir | PEG | 14-16 (%) |