New PDF release: Macromolecular Crystallography Protocols: Volume 2:

New PDF release: Macromolecular Crystallography Protocols: Volume 2:

By Elspeth Garman, Robin L. Owen (auth.), Sylvie Doublié (eds.)

In the last decade on account that book of the 1st version of Crystallographic tools and Protocols the sector has visible a number of significant advancements that experience either sped up the speed of constitution selection and made crystallography obtainable to a broader variety of investigators. quantity I, guidance and Crystallization of Macromolecules is devoted to the crystallization and how one can elevate the chances of acquiring crystals in macromolecules, whereas quantity 2, constitution decision, covers either computational tools for characterizing crystals and fixing structures.

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Extra info for Macromolecular Crystallography Protocols: Volume 2: Structure Determination

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D54, 479–480. 27. Hanson, B. , Schall, C. , and Bunick, G. J. (2003) New techniques in macromolecular cryocrystallography: macromolecular crystal annealing and cryogenic helium. J. Struct. Biol. 142, 77–87. 28. , Caylor, C. , Nonato, M. , Finkelstein, K. , and Thorne, R. E. (2003) Flash-cooling and annealing of protein crystals. Acta Cryst. D58, 459–471. 29. Juers, D. H. and Mathews, B. W. (2004) The role of solvent transport in cryoannealing of macromolecular crystals. Acta Cryst. D60, 412–421.

1). As the Reaction Intermediates in Heme Proteins 23 Table 1 Reaction Scheme for Carbonmonoxymyoglobina Reaction MbCO State: Name: Ligand position A (bound) Heme ⇔ Mb*CO ⇔ B (photolyzed) 1o site Mb**CO ⇔ D (photorelaxed) 2o site Mb + CO S (deoxy) solvent aPhotolysis protocols can drive the ligand to either state B (photolyzed) or state D (photorelaxed), depending on the temperature profile of the sample. Rebinding from B⇒A or B⇒D occurs sequentially. Enthalpies for rebinding are determined using temperature-derivative spectroscopy.

R. Soc. Lond. B 241, 6–8. 8. , Ravelli, R. G. , et al. (2000) Specific chemical and structural damage to proteins produced by synchrotron radiation. PNAS 97, 623–628. 9. Burmeister, W. P. (2000) Structural changes in a cryo-cooled protein crystal owing to radiation damage. Acta Cryst. D56, 328–341. 10. Ravelli, R. G. B. and McSweeney, S. (2000) The ‘fingerprint’ that X-rays can leave on structures. Structure 8, 315–328. 11. Garman, E. (2003) ‘Cool’ crystals: cryocrystallography and radiation damage.

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