3MBO
Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-26 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 41 |
| Unit cell lengths | 226.266, 226.266, 75.354 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.222 - 3.307 |
| R-factor | 0.2293 |
| Rwork | 0.228 |
| R-free | 0.25710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2jjm |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.970 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.360 |
| High resolution limit [Å] | 3.300 | 8.940 | 3.300 |
| Rmerge | 0.169 | 0.085 | 0.919 |
| Number of reflections | 57310 | ||
| <I/σ(I)> | 7.1 | ||
| Completeness [%] | 99.3 | 100 | 93.7 |
| Redundancy | 5.7 | 7.2 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | 15% PEG 3350, 0.2 M MgFormate, 0.02% sodium azide, 1 mM L-malate, 1 mM Uridine diphosphate, pH 7.5, vapor diffusion, hanging drop, temperature 289K |
