WikiSysop: Created page with "== Citation == H. Zhu, G. Terashi, F. Farheen, T. Nakamura, and D. Kihara, “AI-based quality assessment methods for protein structure models from Cryo-EM,” Current Research in Structural Biology, p. 100164, 2025. == Abstract == Cryogenic electron microscopy (cryo-EM) has revolutionized structural biology, with an increasing number of structures being determined by cryo-EM each year, many at higher resolutions. However, challenges remain in accurately interpreting..."

2025-04-14T08:57:44Z

Created page with "== Citation == H. Zhu, G. Terashi, F. Farheen, T. Nakamura, and D. Kihara, “AI-based quality assessment methods for protein structure models from Cryo-EM,” Current Research in Structural Biology, p. 100164, 2025. == Abstract == Cryogenic electron microscopy (cryo-EM) has revolutionized structural biology, with an increasing number of structures being determined by cryo-EM each year, many at higher resolutions. However, challenges remain in accurately interpreting..."

New page

== Citation ==

H. Zhu, G. Terashi, F. Farheen, T. Nakamura, and D. Kihara, “AI-based quality assessment methods for protein structure models from Cryo-EM,” Current Research in Structural Biology, p. 100164, 2025.

== Abstract ==

Cryogenic electron microscopy (cryo-EM) has revolutionized structural biology, with an increasing number of
structures being determined by cryo-EM each year, many at higher resolutions. However, challenges remain in
accurately interpreting cryo-EM maps. Inaccuracies can arise in regions of locally low resolution, where manual
model building is more prone to errors. Validation scores for structure models have been developed to assess both
the compatibility between map density and the structure, as well as the geometric and stereochemical properties
of protein models. Recent advancements have introduced artificial intelligence (AI) into this field. These
emerging AI-driven tools offer unique capabilities in the validation and refinement of cryo-EM-derived protein
atomic models, potentially leading to more accurate protein structures and deeper insights into complex biological
systems.

== Keywords ==

== Links ==

https://www.sciencedirect.com/science/article/pii/S2665928X25000017

== Related software ==

== Related methods ==

== Comments ==

2025Zhu Quality - Revision history