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Additional info for Macromolecular Cyrstallography Protocols Vol.2: Structure Determination (Methods in Molecular Biology Vol 364)
Timm, D. , and Bunick G. J. (1998) Macromolecular crystal annealing: overcoming increased mosaicity associated with cryocrystallography. Acta Cryst. D54, 622–628. 2. Harp, J. , Hanson, B. , Timm, D. , and Bunick, G. J. (1999) Macromolecular crystal annealing: evaluation of techniques and variables. Acta Cryst. D55, 1329–1334. 3. Yeh, J. L. and Hol, W. G. (1998) A flash-annealing technique to improve diffraction limits and lower mosaicity in crystals of glycerol kinase. Acta Cryst. D54, 479–480.
And Mathews, B. W. (2004) The role of solvent transport in cryoannealing of macromolecular crystals. Acta Cryst. D60, 412–421. 2 Determination of Reaction Intermediate Structures in Heme Proteins Kelvin Chu Summary Developments in structural biology and molecular biology have allowed increasingly detailed investigations of structure–function relationships. Although atomic-resolution structures of proteins are becoming more common, a growing number of structural studies have focused on the role played by dynamics and have sought to determine the structure of intermediates in protein reactions.
3. Ultra-Low Temperature Crystallography Crystallographic determination of structures of reaction intermediates relies on either rapid collection via the Laue diffraction or stabilization of intermediates on time-scales suitable for monochromatic data collection (40–42). , by modiﬁcation of the macromolecule, substrate, cofactor, solvent, or pH) or physically (by temperature) (43,44). Because most single-protein crystals are commonly ﬂash cooled for stabilization during data collection to slow radiation damage, trapping intermediates by freeze quenching a reaction is very common.