5DML
Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Oxidized form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9787 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 78.453, 84.463, 85.821 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.386 - 2.452 |
| R-factor | 0.2025 |
| Rwork | 0.202 |
| R-free | 0.21700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q7m |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.262 |
| Data reduction software | XDS (OSX10.9.5_Darwin13.4.0) |
| Data scaling software | Aimless (0.5.8) |
| Phasing software | MOLREP (2.12) |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.390 | 2.540 |
| High resolution limit [Å] | 2.452 | 2.452 |
| Rmerge | 0.096 | 0.597 |
| Number of reflections | 10744 | |
| <I/σ(I)> | 18.19 | 3.69 |
| Completeness [%] | 99.8 | 97.69 |
| Redundancy | 8.1 | 8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293 | 1.6 M ammonium sulphate, 10% v/v glycerol and 0.1 M sodium acetate pH 4.8 |
