ArticleActa crystallographica. Section D, Biological crystallography2015
Experimental phasing for structure determination using membrane-protein crystals grown by the lipid cubic phase method.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Current Developments in Native Nanometric Discoidal Membrane Bilayer Formed by Amphipathic Polymers.Nanomaterials (Basel, Switzerland) · 2021Review
- 3D-printed holders forJournal of applied crystallography · 2020Article
- Structures of human ENT1 in complex with adenosine reuptake inhibitors.Nature structural & molecular biology · 2019Article
- Structural insights into the committed step of bacterial phospholipid biosynthesis.Nature communications · 2017Article
- Introducing site-specific cysteines into nanobodies for mercury labelling allows de novo phasing of their crystal structures.Acta crystallographica. Section D, Structural biology · 2017Article
- The cubicon method for concentrating membrane proteins in the cubic mesophase.Nature protocols · 2017Article
- A Novel Approach to Data Collection for Difficult Structures: Data Management for Large Numbers of Crystals with the BLEND Software.Crystals · 2017Article
- Fast iodide-SAD phasing for high-throughput membrane protein structure determination.Science advances · 2017Article
- X-ray transparent microfluidic chips for high-throughput screening and optimization ofBiomicrofluidics · 2017Article
- A molecular engineering toolbox for the structural biologist.Quarterly reviews of biophysics · 2017Review
- A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes.Acta crystallographica. Section F, Structural biology communications · 2015Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Despite the marked increase in the number of membrane-protein structures solved using crystals grown by the lipid cubic phase or in meso method, only ten have been determined by SAD/MAD. This is likely to be a consequence of the technical difficulties associated with handling proteins and crystals in the sticky and viscous hosting mesophase that is usually incubated in glass sandwich plates for the purposes of crystallization. Here, a four-year campaign aimed at phasing the in meso structure of the integral membrane diacylglycerol kinase (DgkA) from Escherichia coli is reported. Heavy-atom labelling of this small hydrophobic enzyme was attempted by pre-labelling, co-crystallization, soaking, site-specific mercury binding to genetically engineered single-cysteine mutants and selenomethionine incorporation. Strategies and techniques for special handling are reported, as well as the typical results and the lessons learned for each of these approaches. In addition, an assay to assess the accessibility of cysteine residues in membrane proteins for mercury labelling is introduced. The various techniques and strategies described will provide a valuable reference for future experimental phasing of membrane proteins where crystals are grown by the lipid cubic phase method.
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