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 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Top performing articles in Acta Cryst. D, Structural Biology
This virtual collection from Acta Crystallographica Section D, Structural Biology showcases some of the most widely read and highly cited articles in the journal.
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A summary is provided of the last five years of structural studies of bacterial YiiP, providing an overview of how zinc-transporter membrane proteins operate at the molecular level.
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The study of coat protein assemblies on membranes by cryo-electron tomography and subtomogram averaging is discussed, outlining the methodological advancements that enabled the gain of crucial structural insight.
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A long-wavelength mesh data collection using a size-tailored microbeam from concanavalin A microcrystals with linear dimensions of less than 20 µm allowed experimental phase determination using the anomalous signal from naturally occurring Mn2+ and Ca2+ ions.
PDB reference: concanavalin A, 6h2m
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CCP4i2 is a graphical user interface to the CCP4 (Collaborative Computational Project, Number 4) software suite and a Python language framework for software automation.
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A new X-ray diffraction data-analysis package is presented with a description of the algorithms and examples of its application to biological and chemical crystallography.
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Analysing two sequence-related bacterial glycoside hydrolase family 92 mannosidases with distinct functions, a structural basis for their varied specificities is revealed.
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New methods and PHENIX tools for quality assessment of cryo-EM maps, atomic models and model-to-map fitting are presented. Results of systematic application of these tools to high-resolution cryo-EM maps and corresponding atomic models are analyzed and discussed.
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The structural biology of co-translational protein folding on the ribosome is reviewed.
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Experimental phasing of macromolecular crystals is described and explained, with the emphasis on its implementation in the programs SHELXC, SHELXD and SHELXE, which are also used in a number of macromolecular structure-solution pipelines.
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This paper describes different approaches that cryo-EM users can take to improve the quality of their sample distribution and ice for high-resolution single-particle cryo-EM.
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An overview is provided of current crystallographic model validation of proteins and RNA, both foundations and criteria, at all resolution ranges, together with advice on how to correct specific types of problems and when you should not try so hard that you are overfitting.
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Residual OMIT maps can be improved by the selective exclusion of bulk solvent from the OMIT region.
