1E4Y
Mutant P9L of adenylate kinase from E. coli, modified in the Gly-loop
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 279 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.300, 77.800, 57.700 |
| Unit cell angles | 90.00, 94.30, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.850 |
| R-factor | 0.178 |
| Rwork | 0.178 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 3.700 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (1.5) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 |
| High resolution limit [Å] | 3.400 |
| Rmerge | 0.100 |
| Number of reflections | 7261 |
| Completeness [%] | 90.0 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.7 * | 20 * | pH 7.20 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20-25 (mg/ml) | |
| 2 | 1 | drop | Ap5A | 2 (mM) | |
| 3 | 1 | drop | MES | 50 (mM) | |
| 4 | 1 | drop | PEG1500 | 1.5 (%(w/v)) | |
| 5 | 1 | drop | ammonium sulfate | 1.5 (M) | |
| 6 | 1 | reservoir | MES | 50 (mM) | |
| 7 | 1 | reservoir | ammonium sulfate | 2.0-2.2 (M) |
