1GAD
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Experimental procedure
Spacegroup name | C 2 2 21 |
Unit cell lengths | 79.140, 189.560, 122.180 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.197 |
Rwork | 0.197 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.620 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 8.000 | |
High resolution limit [Å] | 1.800 | 1.800 * |
Rmerge | 0.065 * | |
Number of reflections | 66191 * | |
Completeness [%] | 69.0 * | 40 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | tris-sodium citrate | 1.35 (M) | |
2 | 1 | reservoir | EDTA | 1 (mM) | |
3 | 1 | reservoir | dithiothreitol | 1 (mM) | |
4 | 1 | reservoir | azide | 0.1 (mM) | |
5 | 1 | reservoir | NAD | 0.3 (mM) | |
6 | 1 | reservoir | HEPES | 100 (mM) |