1GAE
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 | 79.830, 188.810, 122.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.170 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.480 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 8.000 |
| High resolution limit [Å] | 2.170 |
| Rmerge | 0.066 * |
| Total number of observations | 206671 * |
| Number of reflections | 47343 |
| Completeness [%] | 97.0 |
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) |
