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By Smith E. H.

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Interestingly, this trend could soon start to reverse, as also the home sources are becoming more and more powerful, especially those equipped with advanced micro-focusing optics. Even table-top synchrotrons are now appearing on the market [30]. A high intensity X-ray beam, however, also comes at a price: the higher the intensity, the more serious is the radiation damage that the crystals have to withstand. As a result, crystals quickly loose diffraction power when exposed to synchrotron radiation.

There are, however, some specifics with respect to glycobiological targets, which shall be discussed separately in this section. Let us first consider glycoproteins: proteins to which a carbohydrate chain is covalently attached. Glycoproteins in many cases present a considerable challenge to X-ray structure analysis, because they do not easily form crystals. This is because the attached carbohydrate chains are often heterogenous and flexible and interfere with the formation of crystal contacts.

1. Fungal lectins To date, only few structures of fungal lectins have been solved (Fig. 5). So far, the focus has mainly been on lectins that can be extracted from the fruiting bodies or from the mycelium of mushrooms. These proteins play a role in toxicity, defense mechanisms, and mycorrhization. e. the fucose-binding lectin AAL from the orange peel mushroom Aleuria aurantia, was found to exhibit a six-bladed ␤-propeller fold, different from any lectin fold known before [90]. More recently, a seven-bladed ␤-propeller fold was reported for PVL, a GlcNAc-binding lectin from Psathyrella velutina [91].

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A Bound on the Ratio between the Packing and Covering Densities of a Convex Body by Smith E. H.


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