5DMN
Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Apo form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 85.822, 85.945, 79.016 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.425 - 2.892 |
| R-factor | 0.228 |
| Rwork | 0.226 |
| R-free | 0.27010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q7m |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.923 |
| Data reduction software | XDS (OSX10.9.5_Darwin13.4.0) |
| Data scaling software | Aimless (0.5.8) |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.425 | 2.990 |
| High resolution limit [Å] | 2.892 | 2.892 |
| Rmerge | 0.151 | 0.680 |
| Number of reflections | 13530 | |
| <I/σ(I)> | 11.93 | 3.54 |
| Completeness [%] | 99.7 | 98.41 |
| Redundancy | 6.1 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 1.6 M ammonium sulfate, 10% v/v glycerol and 0.1 M sodium acetate, pH 4.8 |
