1E2K
Kinetics and crystal structure of the wild-type and the engineered Y101F mutant of Herpes simplex virus type 1 thymidine kinase interacting with (North)-methanocarba-thymidine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-12 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 114.000, 117.700, 108.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.700 |
| R-factor | 0.209 * |
| Rwork | 0.209 |
| R-free | 0.25200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vtk |
| RMSD bond length | 0.017 |
| RMSD bond angle | 0.025 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.800 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.050 | 0.580 |
| Number of reflections | 79549 | |
| <I/σ(I)> | 15 | 2.1 |
| Completeness [%] | 99.0 | 99 |
| Redundancy | 4.1 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 23 * | LITHIUM SULFATE, HEPES, DTT, pH 7.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 25 (mg/ml) | |
| 2 | 1 | reservoir | 0.9-1.2 (M) | ||
| 3 | 1 | reservoir | dithiothreitol | 1 (mM) | |
| 4 | 1 | reservoir | HEPES | 0.1 (M) |
