1H94
COMPLEX OF ACTIVE MUTANT (S215->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L.MESENTEROIDES WITH COENZYME NAD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-05-11 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 131.900, 45.200, 93.500 |
| Unit cell angles | 90.00, 107.10, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.213 |
| Rwork | 0.213 |
| R-free | 0.29200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SUBUNIT 'A' OF 1DPG |
| RMSD bond length | 0.006 |
| RMSD bond angle | 22.930 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.600 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.101 * | 0.480 * |
| Total number of observations | 45041 * | |
| Number of reflections | 16682 | 1406 * |
| <I/σ(I)> | 7 | 1.6 |
| Completeness [%] | 88.9 | 81.7 |
| Redundancy | 2.7 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 * | HANGING DROP VAPOUR DIFFUSION, 2+2 MICROLITER DROPS. THE WELL BUFFER: 20% V/V PEG 400 IN 0.1M HEPES-NAOH, PH 7.5 WITH 0.2M CALCIUM CHLORIDE. THE PROTEIN AT 10MG/ML IN 100MM TRIS-HCL WITH 12.5MM NAD+. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG400 | 20 (%(v/v)) | |
| 2 | 1 | reservoir | HEPES-NaOH | 0.1 (M) | |
| 3 | 1 | reservoir | 200 (mM) | ||
| 4 | 1 | drop | protein | 10 (mg/ml) | |
| 5 | 1 | drop | Tris-HCl | 100 (mM) | |
| 6 | 1 | drop | NAD+ | 12.5 (mM) |
