1DRV
ESCHERICHIA COLI DHPR/ACNADH COMPLEX
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 290 |
| Detector technology | AREA DETECTOR |
| Collection date | 1995-09-26 |
| Detector | SIEMENS |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 81.600, 84.600, 91.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.191 * |
| Rwork | 0.191 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | DHPR-NADPH COMPLEX |
| RMSD bond length | 0.018 |
| RMSD bond angle | 20.900 * |
| Data reduction software | SADIE |
| Data scaling software | SAINT |
| Phasing software | AMoRE |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.094 * | |
| Number of reflections | 14402 | |
| <I/σ(I)> | 7.1 | 2.1 |
| Completeness [%] | 87.3 * | 78.1 |
| Redundancy | 3.5 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | Scapin, G., (1995) Biochemistry, 34, 3502. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium salfate | 2.2 (M) | |
| 2 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
| 3 | 1 | drop | protein | 18 (mg/ml) | |
| 4 | 1 | drop | ammonium salfate | 2.2 (M) | |
| 5 | 1 | drop | HEPES | 100 (mM) | |
| 6 | 1 | drop | NADPH | 1.5-2.0 (M) |
