1MDQ
REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN
Experimental procedure
Spacegroup name | C 1 2 1 |
Unit cell lengths | 106.010, 66.460, 57.750 |
Unit cell angles | 90.00, 113.17, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.900 |
R-factor | 0.22 |
Rwork | 0.220 |
RMSD bond length | 0.013 |
RMSD bond angle | 0.033 * |
Phasing software | X-PLOR |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.700 * |
Rmerge | 0.042 * |
Total number of observations | 72712 * |
Number of reflections | 42315 |
Completeness [%] | 78.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.2 * | 4 * | reseeded into drops containing 15% PEG8000, taken from Spurlino, J.C. et al (1991). J. Biol. Chem., 266, 5202-5219. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3.5 (mg/ml) | |
2 | 1 | drop | maltose | 1 (mM) | |
3 | 1 | drop | PEG8000 | 16 (%(w/v)) | |
4 | 1 | drop | sodium azide | 0.02 (%) | |
5 | 1 | drop | sodium citrate | 10 (mM) | |
6 | 1 | reservoir | PEG8000 | 19 (%) |