Tubular Crystals of a Photosystem II Core Complex

Tsiotis, Georgios; Walz, Thomas; Spyridaki, Aspasia; Lustig, Ariel; Engel, Andréas; Ghanotakis, Demetrios F.

doi:10.1006/jmbi.1996.0316

Cited by 49 publications

(34 citation statements)

References 35 publications

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“…Photosystem II is a major protein of the thylakoid membrane of chloroplasts and catalyses the water-splitting reaction associated with photosynthesis. The complex can be divided into the core fraction which comprises approximately 13 polypeptides (Tsiotis et al, 1996) and the antenna fraction containing the light harvesting chlorophyll a/b binding proteins. The solubilized oxygen evolving photosystem II core complex isolated from spinach leaves shows an intrinsic quasi twofold symmetry (Tsiotis et al, 1996;Hasler et al, 1997).…”

Section: Adsorption and Imaging Of Biological Systemsmentioning

confidence: 99%

Adsorption of Biological Molecules to a Solid Support for Scanning Probe Microscopy

Müller

Amrein

Engel

1997

Journal of Structural Biology

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286

204

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Section: Adsorption and Imaging Of Biological Systemsmentioning

confidence: 99%

Adsorption of Biological Molecules to a Solid Support for Scanning Probe Microscopy

Müller

Amrein

Engel

1997

Journal of Structural Biology

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286

204

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“…The mass-per-length is a useful if not essential parameter defining the structure of filaments [25], indicating the number of strands present [26][27][28][29] and in the case of helices restricting the number of possible assembly rules [30][31][32]. Similarly, the massper-area defines the unit cell stoichiometry in 2D crystals or the number of layers in a sheet-like structure [33][34][35][36], information that is otherwise only accessible by chance at their edges, or by atomic force microscopy [36] [37]. Further, in conjunction with a lipid assay by analytical ultracentrifugation mass-per-area measurements can be used to confirm the predicted packing of membrane proteins in two-dimensional crystalline arrays [35].…”

Section: Introductionmentioning

confidence: 99%

“…Similarly, the massper-area defines the unit cell stoichiometry in 2D crystals or the number of layers in a sheet-like structure [33][34][35][36], information that is otherwise only accessible by chance at their edges, or by atomic force microscopy [36] [37]. Further, in conjunction with a lipid assay by analytical ultracentrifugation mass-per-area measurements can be used to confirm the predicted packing of membrane proteins in two-dimensional crystalline arrays [35]. Finally, the presence of an image allows the mass of specific, well defined regions of intact complexes of any shape to be determined and a mass map to be generated [22][23] [38][39][40][41][42][43][44][45].…”

Section: Introductionmentioning

confidence: 99%

Biological Scanning Transmission Electron Microscopy: Imaging and Single Molecule Mass Determination

Müller¹,

Engel²

2006

Chimia

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scanning transmission electron microscopes can both measure the mass of single protein complexes and take amazingly clear images thereof, offering a wide range of applications in structural biology. The principle of mass measurement is presented and discussed and the scope of scanning transmission electron microscopy is illustrated by selected examples. Keywords:Mass determination · scanning transmission electron microscopy · sTEM unstained proteins to be clearly visualised under low dose conditions. Each pixel of the digital image is a quantitative scattering experiment from which the mass of the irradiated volume can be calculated [9]. Thus, the mass of a single protein complex can be determined by integrating over all pixel values that lie within its boundary. The method is applicable to macromolecules of widely varying mass and form (reviewed in [10]). When combined with SDS-gel electrophoresis and, where available, sequence information, STEM mass measurements serve to define protein stoichiometry. Further, as electron energy loss spectroscopy [11][12] or energy dispersive X-ray spectroscopy [13] can be performed while imaging, the STEM also offers the possibility of determining the distribution of specific elements in protein complexes. Indeed the feasibility of mapping single atoms bound to protein molecules has recently been demonstrated [14].The high contrast delivered by the dark-field detector system [15] can also be exploited in negative or positive stain microscopy [16]. Here the STEM yields clear single-shot images that are free from phase contrast fringes. These images frequently provide information only otherwise visible after averaging several hundred projections recorded with a transmission electron microscope (TEM). They thus make it possible to document the presence of distinct protein conformations, information that would be lost by averaging techniques. Indeed, STEM images of both negatively stained [17] and unstained [18] protein complexes have been used to reconstruct their 3D structure.The few dedicated STEMs employed in biology today are invaluable. In particular, the coupling of image and mass gives them the power to answer questions not resolvable by ultracentrifugation or mass spectrometry. Here we discuss the use of the STEM both as an imaging tool and to measure mass, and examine the uncertainties to be expected in STEM mass data sets. The Importance and Versatility of STEM Mass MeasurementsWorldwide, only four laboratories routinely use dedicated STEMs to measure the mass of biological samples. Their facilities are open for external collaborations and the many papers in the literature containing STEM mass measurements document the importance of this rare technique to the scientific community. Although the precision of STEM cannot match that of the mass spectrometer, its capability to measure an enormously wide mass range, its independence from shape assumptions and the presence of an image make the STEM an invaluable tool.The methodology of mass spectrometry has develop...

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“…Many groups are now actively engaged in attempts to determine a high-resolution structure of PSII (Bassi et al, 1989 ;Lyon et al, 1993 ;Tsiotis et al, 1996 ;Hankamer et al, 1997 ;Adir et al, 1998 ;Rhee et al, 1998 ;Zheleva et al, 1998 ;Zouni et al, 1998). Because one of the last major challenges in photosynthesis research is to understand the details of oxygen evolution, it is obvious that the acquisition of detailed structural knowledge on the Mn cluster of PSII is a major priority.…”

Section: The Structure Of Psiimentioning

confidence: 99%

“…The full polypeptide composition of PSII is described in Table 2. The other major approach uses electron microscopy, either with 2D crystals and electron diffraction or by single-particle analysis (Holzenberg et al, 1993 ;Lyon et al, 1993 ;Tsiotis et al, 1996 ;Hankamer et al, 1997Hankamer et al, , 1999Boekema et al, 1998 ;Rhee et al, 1998). The highest-resolution data obtained with 2D crystals so far has recently been presented by Rhee et al (1998), who have produced a three-dimensional reconstruction to a resolution of approx.…”

Section: This Figure Is Reproduced Frommentioning

confidence: 99%

Tansley Review No. 109.

Cogdell

Lindsay

2000

New Phytologist

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This review sets out the case that now is the time for plant science to establish the technologies required for routinely studying the structure and function of plant proteins. The impact that protein structural information can have is illustrated here with reference to photosynthesis. Our understanding of the precise molecular mechanisms of the light-reactions of photosynthesis has been transformed by the combination of high-resolution protein structural data and detailed functional studies. The past few years have been a particularly exciting time to be engaged in basic plant science research. The application of modern techniques of molecular biology has allowed many key questions to be addressed. The stage is now set for an even bigger revolution as the current plant genome sequencing projects are completed. If these advances are going to be fully exploited, plant science must get to grips with studying proteins, not just genes. Reliable methods for the overexpression of proteins in their native state coupled with routine access to structure determination must become the norm rather than the exception. In 1998 there were about 9000 protein structures deposited in the Brookhaven database. Very few of these are plant proteins. This trend will have to be reversed if research in molecular plant science is to fulfil its potential.

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Tubular Crystals of a Photosystem II Core Complex

Cited by 49 publications

References 35 publications

Adsorption of Biological Molecules to a Solid Support for Scanning Probe Microscopy

Adsorption of Biological Molecules to a Solid Support for Scanning Probe Microscopy

Biological Scanning Transmission Electron Microscopy: Imaging and Single Molecule Mass Determination

Tansley Review No. 109.

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