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Crystallisation of CP43, a chlorophyll binding protein of photosystem II: an electron microscopy analysis of molecular packing.

Abstract：

:Microcrystals of the chlorophyll binding protein, CP43, isolated from spinach thylakoid membranes have been studied by electron microscopy both in negative stain and in vitreous ice. Image analyses of three characteristic views show that the crystals are built of five different layers perpendicular to the c-axis. Each layer consists of different orientations of the CP43 protein. The unit cell derived from the end-on view (looking down the c-axis) shows an angle of 120 degrees, suggesting a threefold rotational symmetry. Both negative staining and cryo data are consistent with a hexagonal crystal lattice. Interpretation of the arrangement of the CP43 protein within this crystal lattice can be made based on 8- and 9-A electron crystallographic structures previously published that provide a model for the organisation of the transmembrane helices of CP43. Overall the analysis presented is consistent with X-ray diffraction data obtained from larger CP43 crystals and forms a framework on which to base further structural studies of this chlorophyll binding protein.

journal_name

J Struct Biol

journal_title

Journal of structural biology

authors

Büchel C,Morris E,Barber J

doi

10.1006/jsbi.2000.4294

keywords:

subject

Has Abstract

pub_date

2000-09-01 00:00:00

pages

181-6

issue

3

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(00)94294-1

journal_volume

131

pub_type

杂志文章

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