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7A projection map of the S-layer protein sbpA obtained with trehalose-embedded monolayer crystals.

Abstract：

:Two-dimensional crystallization on lipid monolayers is a versatile tool to obtain structural information of proteins by electron microscopy. An inherent problem with this approach is to prepare samples in a way that preserves the crystalline order of the protein array and produces specimens that are sufficiently flat for high-resolution data collection at high tilt angles. As a test specimen to optimize the preparation of lipid monolayer crystals for electron microscopy imaging, we used the S-layer protein sbpA, a protein with potential for designing arrays of both biological and inorganic materials with engineered properties for a variety of nanotechnology applications. Sugar embedding is currently considered the best method to prepare two-dimensional crystals of membrane proteins reconstituted into lipid bilayers. We found that using a loop to transfer lipid monolayer crystals to an electron microscopy grid followed by embedding in trehalose and quick-freezing in liquid ethane also yielded the highest resolution images for sbpA lipid monolayer crystals. Using images of specimens prepared in this way we could calculate a projection map of sbpA at 7A resolution, one of the highest resolution projection structures obtained with lipid monolayer crystals to date.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Norville JE,Kelly DF,Knight TF Jr,Belcher AM,Walz T

doi

10.1016/j.jsb.2007.06.002

subject

Has Abstract

pub_date

2007-12-01 00:00:00

pages

313-23

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(07)00140-2

journal_volume

160

pub_type

杂志文章

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