4MNR
Crystal Structure of D,D-Transpeptidase Domain of Peptidoglycan Glycosyltransferase from Eggerthella lenta
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-12-18 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97895 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.060, 69.159, 119.975 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.091 - 1.653 |
R-factor | 0.165 |
Rwork | 0.164 |
R-free | 0.18400 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.079 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | PHENIX ((phenix.refine: dev_1367)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.680 |
High resolution limit [Å] | 1.630 | 1.630 |
Number of reflections | 48312 | |
<I/σ(I)> | 10.1 | 1.9 |
Completeness [%] | 99.5 | 96.2 |
Redundancy | 3.9 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 0.2 M calcium acetate, 0.1 M imidazole pH 8.0, 20 %(w/v) PEG1000, VAPOR DIFFUSION, SITTING DROP, temperature 289K |