REVIEW 1 cited by
Cross-Modal Fusion Between Data in SAXS and Cryo-EM for Biomolecular Structure Determination
Not yet reviewed by Pith; the record is open.
This paper has not been read by Pith yet. Machine review is queued; the pith claim, tier, and objections will appear here once it completes.
SPECIMEN: schema-true, not a live event
T0 review · schema-true
One-sentence machine reading of the paper's core claim.
pith:XXXXXXXX · record.json · timestamp
read the original abstract
Cryo-Electron Microscopy (cryo-EM) has become an extremely powerful method for resolving structural details of large biomolecular complexes. However, challenging problems in single-particle methods remain open because of (1) the low signal-to-noise ratio in EM; and (2) the potential anisotropy and lack of coverage of projection directions relative to the body-fixed coordinate system for some complexes. Whereas (1) is usually addressed by class averaging (and increasingly due to rapid advances in microscope and sensor technology), (2) is an artifact of the mechanics of interaction of biomolecular complexes and the vitrification process. In the absence of tilt series, (2) remains a problem, which is addressed here by supplementing EM data with Small-Angle X-Ray Scattering (SAXS). Whereas SAXS is of relatively low resolution and contains much lower information content than EM, we show that it is nevertheless possible to use SAXS to fill in blind spots in EM in difficult cases where the range of projection directions is limited.
Forward citations
Cited by 1 Pith paper
-
Two Datasets Are Better Than One: Method of Double Moments for 3-D Reconstruction in Cryo-EM
A bandlimited 3-D structure is uniquely determined, up to rotation and reflection, by one uniform-dataset second moment plus a second non-uniform dataset's second moment.
Discussion (0). Continue with ORCID to comment.