5DMM
Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Metallated 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) | 0.9787 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 78.949, 85.924, 87.662 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.225 - 1.779 |
| R-factor | 0.1841 |
| Rwork | 0.183 |
| R-free | 0.20520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q7m |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.119 |
| Data reduction software | XDS (Darwin 13.4.0) |
| Data scaling software | Aimless (0.5.8) |
| Phasing software | MOLREP (2.12) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.230 | 1.840 |
| High resolution limit [Å] | 1.779 | 1.779 |
| Rmerge | 0.093 | 0.660 |
| Number of reflections | 13523 | |
| <I/σ(I)> | 14.86 | 2.49 |
| Completeness [%] | 93.4 | 95.36 |
| Redundancy | 5.2 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 1.6 M ammonium sulphate, 10% v/v glycerol and 0.1 M sodium acetate pH 4.8 |
