3G2M
Crystal Structure of the Glycopeptide N-methyltransferase MtfA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-17 |
Wavelength(s) | 0.9800 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 127.443, 71.682, 75.189 |
Unit cell angles | 90.00, 103.02, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.239 |
Rwork | 0.238 |
R-free | 0.27100 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.054 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
Rmerge | 0.046 | 0.037 | 0.315 |
Number of reflections | 45124 | ||
<I/σ(I)> | 20.585 | ||
Completeness [%] | 97.4 | 99.1 | 84.6 |
Redundancy | 2.5 | 2.6 | 2.2 |
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 |