.png){kind=icon}
.png){kind=icon}
Return
Fast native-SAD phasing for routine macromolecular structure determination
.png){kind=icon}
PRE
AI
DOI：10.1038/nmeth.3211.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.
Keywords:
ANOMALOUS DIFFRACTION
REFINEMENT
GENOMICS
AI Summary
Key information extracted from the uploaded paper, including a brief overview, abstract, background, key highlights, visual analysis, and future outlook.
Journal
IF:
32.1
Papers:
7.2K
Citations:
12.7W
View more organizations