12EM
Crystal structure of a B1,3-Glucosyltransferase (B3GLCT) reveals an unusual mode of substrate recognition by a two-domain GT-A fold glycosyltransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-06-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 133.910, 133.910, 137.810 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 57.980 - 2.070 |
| R-factor | 0.2006 |
| Rwork | 0.199 |
| R-free | 0.22610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.091 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.21_5207: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.980 | 2.180 |
| High resolution limit [Å] | 2.060 | 2.060 |
| Number of reflections | 45560 | 7200 |
| <I/σ(I)> | 21.1 | |
| Completeness [%] | 99.8 | 99.3 |
| Redundancy | 18.2 | |
| CC(1/2) | 0.999 | 0.548 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 34% PEG 3350, 0.2 M dibasic ammonium phosphate and 0.5 M betaine |
