6H9E
Structure of glutamate mutase reconstituted with homo-coenzyme B12
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-02-05 |
Detector | MARRESEARCH |
Wavelength(s) | 0.8428 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.890, 112.620, 108.350 |
Unit cell angles | 90.00, 95.69, 90.00 |
Refinement procedure
Resolution | 40.410 - 1.820 |
R-factor | 0.1384 |
Rwork | 0.137 |
R-free | 0.16750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ccw |
RMSD bond length | 0.007 |
RMSD bond angle | 0.844 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHENIX |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.410 | 1.890 |
High resolution limit [Å] | 1.820 | 1.820 |
Rmerge | 0.052 | 0.299 |
Rmeas | 0.064 | 0.366 |
Rpim | 0.035 | 0.207 |
Number of reflections | 130639 | 12636 |
<I/σ(I)> | 19.5 | 4.5 |
Completeness [%] | 96.1 | 93.7 |
Redundancy | 3 | 2.8 |
CC(1/2) | 0.998 | 0.915 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 6% (w/v) PEG-4000, 0.1 M DL-tartrate, pH=4.5, 2 mM CdCl2 |