Macromolecular Cryocrystallography

Garman, Elspeth F.; Schneider, Thomas R.

doi:10.1107/s0021889897002677

Cited by 338 publications

(296 citation statements)

References 141 publications

(222 reference statements)

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“…In this technique, protein crystals are 'flash cooled' to near liquid-nitrogen temperature, and their diffraction data collected at ca. 100 K (Garman & Schneider 1997) or 35 K (Nakasako et al 2002a). In flash cooling of protein crystals, water molecules rapidly lose their kinetic energies and are frozen into the vitreous state.…”

Section: Cryogenic X-ray Crystallography As a Tool For Investigating mentioning

confidence: 99%

“…In the past decade, cryogenic techniques in X-ray diffraction experiments have been routinely and widely used to overcome radiation damage to protein crystals, in particular the use of intense synchrotron X-rays (Garman & Schneider 1997). In this technique, protein crystals are 'flash cooled' to near liquid-nitrogen temperature, and their diffraction data collected at ca.…”

Section: Cryogenic X-ray Crystallography As a Tool For Investigating mentioning

confidence: 99%

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Water–protein interactions from high–resolution protein crystallography

Nakasako

2004

Phil. Trans. R. Soc. Lond. B

163

119

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To understand the role of water in life at molecular and atomic levels, structures and interactions at the protein-water interface have been investigated by cryogenic X-ray crystallography. The method enabled a much clearer visualization of definite hydration sites on the protein surface than at ambient temperature. Using the structural models of proteins, including several hydration water molecules, the characteristics in hydration structures were systematically analysed for the amount, the interaction geometries between water molecules and proteins, and the local and global distribution of water molecules on the surface of proteins. The tetrahedral hydrogen-bond geometry of water molecules in bulk solvent was retained at the interface and enabled the extension of a three-dimensional chain connection of a hydrogen-bond network among hydration water molecules and polar protein atoms over the entire surface of proteins. Networks of hydrogen bonds were quite flexible to accommodate and/or to regulate the conformational changes of proteins such as domain motions. The present experimental results may have profound implications in the understanding of the physico-chemical principles governing the dynamics of proteins in an aqueous environment and a discussion of why water is essential to life at a molecular level.

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Section: Cryogenic X-ray Crystallography As a Tool For Investigating mentioning

confidence: 99%

Section: Cryogenic X-ray Crystallography As a Tool For Investigating mentioning

confidence: 99%

Water–protein interactions from high–resolution protein crystallography

Nakasako

2004

Phil. Trans. R. Soc. Lond. B

163

119

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“…The time-dependent temperature is averaged over the middle one-third of the crystal volume (Halle 2004). 200 K below the physiological temperature range (Garman 2003). Cryocrystallography evolved primarily as a means to combat radiation damage to crystals from intense synchrotron X-ray beams, based on the idea that radiation-induced free radicals cannot damage the biomolecule once they are trapped in the vitrified bulk solvent within the crystal (Garman & Schneider 1997). The insufficiently appreciated price for this protection is the introduction of structural cryo-artefacts.…”

Section: Structure Of Protein Hydrationmentioning

confidence: 99%

Protein hydration dynamics in solution: a critical survey

Halle

2004

Phil. Trans. R. Soc. Lond. B

492

576

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The properties of water in biological systems have been studied for well over a century by a wide range of physical techniques, but progress has been slow and erratic. Protein hydration-the perturbation of water structure and dynamics by the protein surface-has been a particularly rich source of controversy and confusion. Our aim here is to critically examine central concepts in the description of protein hydration, and to assess the experimental basis for the current view of protein hydration, with the focus on dynamic aspects. Recent oxygen-17 magnetic relaxation dispersion (MRD) experiments have shown that the vast majority of water molecules in the protein hydration layer suffer a mere twofold dynamic retardation compared with bulk water. The high mobility of hydration water ensures that all thermally activated processes at the protein-water interface, such as binding, recognition and catalysis, can proceed at high rates. The MRD-derived picture of a highly mobile hydration layer is consistent with recent molecular dynamics simulations, but is incompatible with results deduced from intermolecular nuclear Overhauser effect spectroscopy, dielectric relaxation and fluorescence spectroscopy. It is also inconsistent with the common view of hydration effects on protein hydrodynamics. Here, we show how these discrepancies can be resolved.

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Section: Introductionmentioning

confidence: 99%

“…In many cases, a dramatic reduction in radiation damage at low temperatures allows complete data sets to be collected from a single crystal. cryoprotectors make it possible to cool samples to low temperature and store them without damage in the crystal [5].In this article ice formation is investigated by small-and wide-angle X-ray scattering (SAXS and WAXS) in ternary phospholipid/cryoprotector/water systems. Three phospholipids are studied: dimyristoylphosphatidylcholine (DMPC), dipalmitoylphosphatidylcholine (DPPC) and distearoylphosphatidylcholine (DSPC).…”

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confidence: 99%

Ice formation in model biological membranes in the presence of cryoprotectors

Киселев

Lesieur

Kisselev

et al. 2000

Nuclear Instruments and Methods in Physics Research Section A:

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Ice formation in model biological membranes is studied by SAXS and WAXS in the presence of cryoprotectors: dimethyl sulfoxide and glycerol. Three types of phospholipid membranes: DPPC, DMPC, DSPC are chosen for the investigation as well-studied model biological membranes. A special cryostat is used for sample cooling from 14.1 o C to −55.4 o C. The ice formation is only detected by WAXS in binary phospholipid/water and ternary phospholipid/cryoprotector/water systems in the condition of excess solvent. Ice formation in a binary phospholipid/water system creates an abrupt decrease of the membrane repeat distance by ∆d, so-called ice-induced dehydration of intermembrane space. The value of ∆d decreases as the cryoprotector concentration increases. The formation of ice does not influence the membrane structure (∆d = 0) for cryoprotector mole fractions higher than 0.05. IntroductionDimethyl sulfoxide (DMSO) and glycerol are well-known cryoprotectors widely used in cryobiology for the conservation of biological tissues at low temperatures [1]. The main purpose of cryobiology is to find an "optimal" way for cooling biological systems to low temperatures (about the liquid nitrogen temperature), and prevent the crystallisation of water inside biological tissues. One of the problems is a longer time of freeze-induced dehydration (diffusion of water molecules from biological tissues through the membrane to the conserving solvent) than the time of ice formation [2]. The ice-induced dehydration of intermembrane space at the moment of water crystallization is observed by X-ray diffraction [3] and calorimetry [4] for binary phospholipid /water systems. In macromolecular crystallography the portion of X-ray diffraction experiments at cryogenic temperatures is exponentially increasing. In many cases, a dramatic reduction in radiation damage at low temperatures allows complete data sets to be collected from a single crystal. cryoprotectors make it possible to cool samples to low temperature and store them without damage in the crystal [5].In this article ice formation is investigated by small-and wide-angle X-ray scattering (SAXS and WAXS) in ternary phospholipid/cryoprotector/water systems. Three phospholipids are studied: dimyristoylphosphatidylcholine (DMPC), dipalmitoylphosphatidylcholine (DPPC) and distearoylphosphatidylcholine (DSPC). DPPC, DMPC, and DSPC are taken as phospholipids with an equal polar heads and with the difference in the length of hydrocarbon chains. The reason why we use DMSO and glycerol is the fact of their different interactions with the membrane surface. Glycerol penetrates into the region of polar head groups and produces influence on the thickness of the membrane bilayer and the thickness of an intermembrane solvent [6]. DMSO molecules do not penetrate into the region of polar head groups and thus do not influence the membrane thickness [7,8]. DMSO molecules strongly interact with water molecules and form hydrogen bonds. Such interaction is more intensive than the interaction between DMSO a...

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Macromolecular Cryocrystallography

Cited by 338 publications

References 141 publications

Water–protein interactions from high–resolution protein crystallography

Water–protein interactions from high–resolution protein crystallography

Protein hydration dynamics in solution: a critical survey

Ice formation in model biological membranes in the presence of cryoprotectors

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