Tubular Crystals of a Photosystem II Core Complex

An oxygen evolving photosystem II core complex containing all three extrinsic proteins (33, 23, 17 kDa) was isolated from spinach and reconstituted into tubular two-dimensional crystals of 72.9 nm diameter and 1–2 micrometers length. While the 17 and 23 kDa polypeptides were lost during crystallizat...

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Bibliographic Details
Published in:Journal of molecular biology 1996-06, Vol.259 (2), p.241-248
Main Authors: Tsiotis, Georgios, Walz, Thomas, Spyridaki, Aspasia, Lustig, Ariel, Engel, Andreas, Ghanotakis, Demetrios
Format: Article
Language:English
Subjects:
2D crystals
33 kDa protein
Crystallization
crystals
Dimyristoylphosphatidylcholine - pharmacology
electron microscopy
Image Processing, Computer-Assisted
immuno-gold labeling
immunoelectron microscopy
molecular conformation
oxygen evolving complex
Photosynthetic Reaction Center Complex Proteins - chemistry
Photosynthetic Reaction Center Complex Proteins - drug effects
Photosynthetic Reaction Center Complex Proteins - ultrastructure
photosystem II
Photosystem II Protein Complex
plant proteins
Spinacia oleracea
Spinacia oleracea - chemistry
structure
ultrastructure
X-ray diffraction
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Description
Summary:An oxygen evolving photosystem II core complex containing all three extrinsic proteins (33, 23, 17 kDa) was isolated from spinach and reconstituted into tubular two-dimensional crystals of 72.9 nm diameter and 1–2 micrometers length. While the 17 and 23 kDa polypeptides were lost during crystallization, the extrinsic 33 kDa protein was retained. The optical spectrum of the crystallized core was characteristic of an intact PSII core complex. Immunoelectron microscopy revealed that the lumenal surface of the PSII complex was exposed at the outside of the cylindrical tubes. The projection of the complex was determined from flattened tubular crystals by negative stain electron microscopy and image analysis to 2.0 nm resolution. Rhombic unit cells ( a=16.2 nm, b=13.7 nm; γ=142.4°) contained one PSII complex.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1996.0316