ArticleActa crystallographica. Section D, Structural biology2025
Useful experimental aspects of small-wedge synchrotron crystallography for accurate structure analysis of protein molecules.
Article in Acta crystallographica. Section D, Structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Enhanced intensity-based clustering of isomorphous multi-crystal data sets in the presence of subtle variations.Acta crystallographica. Section D, Structural biology · 2025Article
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Abstract
Recent advances in low-emittance synchrotron X-ray technology and highly sensitive photon-counting detectors have revolutionized protein micro-crystallography in structural biology. These developments and improvements to sample-exchange robots and beamline control have paved the way for automated and efficient unattended data collection. This study analyzed protein crystal structures such as type 2 angiotensin II receptor, CNNM/CorC membrane proteins and polyhedral protein crystals using small-wedge synchrotron crystallography (SWSX), which dramatically improves measurement efficiency through automated measurement. We evaluated the data quality using SWSX, focusing on `massive data collection'. In this context, `massive' refers to data sets with a multiplicity exceeding 100. The findings could potentially lead to the development of more efficient experimental conditions, such as obtaining high-resolution data using a smaller number of crystals. We have demonstrated that the application of machine learning, a modern key component of data science, to classify data groups is an integral part of the analysis process and may play a crucial role in improving data quality. These results indicate that SWSX is one of the essential candidates for crystal structure analysis methods for difficult-to-analyze samples: it can enable diverse and complex protein functional analysis.
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