Literature DB >> 14573950

Is it jolly SAD?

Eleanor Dodson1.   

Abstract

Examples of phasing macromolecular crystal structures based on single-wavelength anomalous dispersion (SAD) have demonstrated that this approach may have general applications in structural biology. With better data-collection facilities and cryogenic techniques, combined with powerful data-processing, phasing and density-modification programs, the SAD approach may prove simpler than phasing from multi-wavelength (MAD) measurements. It can be performed at any wavelength where anomalous scattering can be observed, in many cases using laboratory X-ray sources. However, there is still a need for accurate data, successful phase improvement and a certain amount of luck. This paper extends the discussion of Jolly SAD in Dauter et al. [Dauter, Z., Dauter, M. & Dodson, E. (2002), Acta Cryst. D58, 494-506].

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Year:  2003        PMID: 14573950     DOI: 10.1107/s0907444903020936

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  15 in total

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3.  Approaches to automated protein crystal harvesting.

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5.  The use of Co2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein.

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6.  Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.

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8.  Introduction to phasing.

Authors:  Garry L Taylor
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2010-03-24

9.  Carrying out an optimal experiment.

Authors:  Zbigniew Dauter
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Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2010-03-24
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