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5 citations found for Robinson, A
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The title compound, C18H28N2, with a crystallographic twofold rotation axis, can function as a C2-symmetric diamine ligand.
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The nature of crystallography of biological macromolecules can be unpredictable, and protein crystals do not consistently produce high-resolution diffraction data. In the study described here, it was sought to develop a computational design approach that could identify resolution-enhancing point mutations at crystallographic protein–protein interfaces.
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The structure of the DLH (C123S) with PMS bound indicates that the reason the enzyme is able to catalyse a wide range of dissimilar substrates is a consequence of its capacity to undergo a coordinated restructuring of the active site and associated regions of the molecule without compromising the stability of its tertiary fold.
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Given the tunability of synchrotron radiation, photoemission spectroscopy can be used to monitor the growth modes of thin films in UHV. Cross-section effects such as Cooper minima and resonant photoemission can be exploited to maximize the adsorbate signal and minimize that from the substrate. Under favourable circumstances growth can be monitored in real time at coverages of <1%. As an example the growth of Gd on W(110) is investigated.