Abstract
Determination in the past and the contemporary re-determination of several protein structures are considered in the context of our personal experience with the use of single-wavelength anomalous dispersion (SAD) techniques. A unifying feature of these cases is that in each event, the anomalous signal generated by metal ions was not optimized to the peak of the absorption edge, but was, nevertheless sufficient for structure re-determination. Examples are described with the emphasis on educational aspects. Determinants of success are discussed in each case. In addition, briefly discussed are some concepts related to the quality of the diffraction data used in experimental phasing, with special attention to SAD phasing.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Derewenda Z, Yariv J, Helliwell JR, Kalb AJ, Dodson EJ, Papiz MZ, Wan T, Campbell J (1989) The structure of the saccharide-binding site of concanavalin A. EMBO J 8:2189–2193
Emsley P, Lohkamp B, Scott WG, Cowtan K (2010) Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66:486–501
Frolow F, Kalb AJ, Yariv J (1994) Structure of a unique twofold symmetric haem-binding site. Nat Struct Biol 1:453–460
Frolow F, Harel M, Sussman JL, Mevarech M, Shoham M (1996) Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nat Struct Biol 3:452–458
Furey W, Swaminathan S (1997) PHASES-95: a program package for processing and analyzing diffraction data from macromolecules. Methods Enzymol 277:590–620
Jones TA (1985) Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol 115:157–171
Minor W, Cymborowski M, Otwinowski Z, Chruszcz M (2006) HKL-3000: the integration of data reduction and structure solution–from diffraction images to an initial model in minutes. Acta Crystallogr D Biol Crystallogr 62:859–866
Naismith JH, Emmerich C, Habash J, Harrop SJ, Helliwell JR, Hunter WN, Raftery J, Kalab AJ, Yariv J (1994) Refined structure of concanavalin A complexed with methyl alpha-D-mannopyranoside at 2.0 A resolution and comparison with the saccharide-free structure. Acta Crystallogr D Biol Crystallogr 50:847–858
Sheldrick GM (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr 66:479–485
Sumner JB (1919) The Globulins of the Jack Bean, Canavalia ensiformis. J Biol Chem 37:137–142
Yaniv O, Halfon Y, Shimon LJ, Bayer EA, Lamed R, Frolow F (2012) Structure of CBM3b of the major cellulosomal scaffoldin subunit ScaA from Acetivibrio cellulolyticus. Acta Crystallogr Sect F Struct Biol Cryst Commun 68:8–13
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer Science+Business Media Dordrecht
About this paper
Cite this paper
Frolow, F. (2013). Use of a Weak Anomalous Signal for Phasing in Protein Crystallography: Reflection from Personal Experience. In: Read, R., Urzhumtsev, A., Lunin, V. (eds) Advancing Methods for Biomolecular Crystallography. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6232-9_16
Download citation
DOI: https://doi.org/10.1007/978-94-007-6232-9_16
Published:
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-007-6231-2
Online ISBN: 978-94-007-6232-9
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)