ArticleAdvances in experimental medicine and biology2016
Applications of the BLEND Software to Crystallographic Data from Membrane Proteins.
Article in Advances in experimental medicine and biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- The CNK-HYP scaffolding complex promotes RAF activation by enhancing KSR-MEK interaction.Nature structural & molecular biology · 2024Article
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.Nature communications · 2022Article
- Structural basis for C-type inactivation in a Shaker family voltage-gated KScience advances · 2022Article
- Versatile microporous polymer-based supports for serial macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2021Article
- A Novel Approach to Data Collection for Difficult Structures: Data Management for Large Numbers of Crystals with the BLEND Software.Crystals · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
X-ray diffraction from crystals of membrane proteins very often yields incomplete datasets due to, among other things, severe radiation damage. Multiple crystals are thus required to form complete datasets, provided the crystals themselves are isomorphous. Selection and combination of data from multiple crystals is a difficult and tedious task that can be facilitated by purpose-built software. BLEND, in the CCP4 suite of programs for macromolecular crystallography (MX), has been created exactly for this reason. In this chapter the program is described and its workings illustrated by means of data from two membrane proteins.
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