Expression, Purification, and Crystallization of Full-Length HSV-1 gB for Structure Determination

Cooper, Rebecca S.; Heldwein, Ekaterina E.

doi:10.1007/978-1-4939-9814-2_24

Cited by 1 publication

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References 27 publications

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“…(2014), and Chapter 11 in Popot, 2018). Indeed, a recent study has shown that a mix of DDM and A8-35 (the latter used as a stabilizing agent) allows one to solve the X-ray structure of herpes simplex virus glycoprotein B at a higher resolution than can be achieved with DDM alone (Cooper et al ., 2018; Cooper and Heldwein, 2020). More to the point is the fact that early APols carried charged polar moieties, which tend to hamper 3D crystallization, whereas non-ionic APols (NAPols) (Bazzacco et al ., 2012) have only recently become commercially available.…”

Section: An Overview Of Surfactant Usage At the Vitrification Stepmentioning

confidence: 99%

Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy

Bon

Michon

Popot

et al. 2021

Quart. Rev. Biophys.

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Over the past decade, the structural biology of membrane proteins (MPs) has taken a new turn thanks to epoch-making technical progress in single-particle electron cryo-microscopy (cryo-EM) as well as to improvements in sample preparation. The present analysis provides an overview of the extent and modes of usage of the various types of surfactants for cryo-EM studies. Digitonin, dodecylmaltoside, protein-based nanodiscs, lauryl maltoside-neopentyl glycol, glyco-diosgenin, and amphipols (APols) are the most popular surfactants at the vitrification step. Surfactant exchange is frequently used between MP purification and grid preparation, requiring extensive optimization each time the study of a new MP is undertaken. The variety of both the surfactants and experimental approaches used over the past few years bears witness to the need to continue developing innovative surfactants and optimizing conditions for sample preparation. The possibilities offered by novel APols for EM applications are discussed.

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Section: An Overview Of Surfactant Usage At the Vitrification Stepmentioning

confidence: 99%

Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy

Bon

Michon

Popot

et al. 2021

Quart. Rev. Biophys.

View full text Add to dashboard Cite

show abstract

Expression, Purification, and Crystallization of Full-Length HSV-1 gB for Structure Determination

Cited by 1 publication

References 27 publications

Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy

Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy

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