1QKJ
T4 Phage B-Glucosyltransferase, Substrate Binding and Proposed Catalytic Mechanism
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM02 |
| Synchrotron site | ESRF |
| Beamline | BM02 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.460, 102.470, 59.420 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.198 * |
| Rwork | 0.190 |
| R-free | 0.29000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bgu |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.682 * |
| Phasing software | X-PLOR (3.84) |
| Refinement software | X-PLOR (3.84) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | |
| High resolution limit [Å] | 2.300 | |
| Rmerge | 0.041 * | 0.230 * |
| Total number of observations | 57848 * | |
| Number of reflections | 16930 | |
| Completeness [%] | 96.0 | 78 * |
| Redundancy | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | pH 7.40 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG4000 | 10 (%(w/v)) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | protein | 1 (mM) | |
| 4 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
| 5 | 1 | reservoir | ammonium sulfate | 52 (%sat) | |
| 6 | 1 | reservoir | MES | 0.1 (M) |
