3G2O
Crystal Structure of the Glycopeptide N-methyltransferase MtfA complexed with (S)-adenosyl-L-methionine (SAM)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-06-17 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9798 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 126.917, 72.335, 75.306 |
| Unit cell angles | 90.00, 103.89, 90.00 |
Refinement procedure
| Resolution | 42.370 - 2.100 |
| R-factor | 0.218 |
| Rwork | 0.216 |
| R-free | 0.24500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3g2m |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 4.520 | 2.100 |
| Rmerge | 0.040 | 0.023 | 0.276 |
| Number of reflections | 35055 | ||
| <I/σ(I)> | 26.008 | ||
| Completeness [%] | 90.8 | 93.3 | 60.9 |
| Redundancy | 3.5 | 3.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 294 | 0.1M MES pH 6.5, 18% PEG-monomethyl ether 5K, vapor diffusion, hanging drop, temperature 294K |
