Greatly reduced radiation damage in ribonuclease crystals mounted on glass fibers

Dewan, John C.; Tilton, Robert D.

doi:10.1107/s0021889887087004

Cited by 26 publications

(21 citation statements)

References 11 publications

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“…This was realized first by Haas & Rossman (1970). Later, radiation damage was found to be undetectable in a number of experiments performed at cryogenic temperatures, and it was found possible to collect complete data sets from a single crystal (Dewan & Tilton, 1987;Hope, Frolow, yon B6hlen, Makowski, Kratky, Halfon, Danz, Webster, Bartels & Yonath, 1989;Young, Dewan, Thompson & Nave, 1990;Gonzales, Thompson & Nave, 1992;Young, Dewan & Tilton, 1993). In addition to eliminating atomic diffusion, the rigid solvent matrix provides a scaffold against the spreading of damage via 'domino effects' mediated by lattice contacts (Henderson, 1990).…”

Section: Radiation Damagementioning

confidence: 99%

“…Dewan et al (Dewan & Tilton, 1987) have used this method for mounting protein crystals. An extension of it was pioneered by Hope (1988), in which the protein crystals are coated in oil, to prevent dehydration, prior to being placed onto a standard smallmolecule-type glass fibre soldered into a copper pin for flash cooling.…”

Section: Crystal-mounting Instrumentationmentioning

confidence: 99%

See 1 more Smart Citation

Macromolecular Cryocrystallography

Garman¹,

Schneider²

1997

J Appl Crystallogr

345

289

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The current techniques for X-ray-diffraction data collection from macromolecular crystals at cryogenic temperatures are reviewed. The development of the experimental methods is outlined and the basic concepts pertaining to radiation damage and cryoprotection are summarized. Emphasis is placed on the practical aspects important to the success of the techniques, and a detailed account of these is presented.

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Section: Radiation Damagementioning

confidence: 99%

Section: Crystal-mounting Instrumentationmentioning

confidence: 99%

Macromolecular Cryocrystallography

Garman¹,

Schneider²

1997

J Appl Crystallogr

345

289

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“…Therefore, the method of shock-freezing (Dewan & Tilton, 1987;Hope, 1988Hope, , 1990 was used. For all low-temperature data sets, crystals were fixed on the tip of a thin glass fiber by a ball of epoxy cement.…”

Section: Crystal Preparation and Data Collectionmentioning

confidence: 99%

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water

Kurinov¹,

Harrison²

1995

Acta Crystallogr D Biol Crystallogr

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Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 A. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was discontinuous with the volume being near 238 000 A, 3 from 295 to 250 K and about 220200 A 3 below 180 K. The thermal expansion of the protein has been analyzed and shows anisotropy, which is correlated with local atomic packing and secondarystructure elements. The lysozyme structure at low temperature is nearly the same as that at high temperature, with only small relative translations and rotations of structure elements including a hingebending rearrangement of two domains. Because of a considerable increase of lattice disorder at low temperature dynamical analysis of internal motion is difficult. The analysis of structural and dynamical properties of well ordered protein-bound water has been carried out.

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“…Most macromolecular crystal structures are now determined at cryogenic temperature ($100 K) as a way of limiting the radiation damage to the crystal during the diffraction experiment (Low et al, 1966;Haas & Rossmann, 1970;Dewan & Tilton, 1987;Hope, 1988). However, it is common for the cooling process to disrupt the crystal order and decrease the diffraction quality.…”

Section: Introductionmentioning

confidence: 99%

Progress in rational methods of cryoprotection in macromolecular crystallography

Alcorn

Juers

2010

Acta Crystallogr D Biol Crystallogr

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Cryogenic cooling of macromolecular crystals is commonly used for X-ray data collection both to reduce crystal damage from radiation and to gather functional information by cryogenically trapping intermediates. However, the cooling process can damage the crystals. Limiting cooling-induced crystal damage often requires cryoprotection strategies, which can involve substantial screening of solution conditions and cooling protocols. Here, recent developments directed towards rational methods for cryoprotection are described. Crystal damage is described in the context of the temperature response of the crystal as a thermodynamic system. As such, the internal and external parts of the crystal typically have different cryoprotection requirements. A key physical parameter, the thermal contraction, of 26 different cryoprotective solutions was measured between 294 and 72 K. The range of contractions was 2-13%, with the more polar cryosolutions contracting less. The potential uses of these results in the development of cryocooling conditions, as well as recent developments in determining minimum cryosolution soaking times, are discussed.

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Greatly reduced radiation damage in ribonuclease crystals mounted on glass fibers

Cited by 26 publications

References 11 publications

Macromolecular Cryocrystallography

Macromolecular Cryocrystallography

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water

Progress in rational methods of cryoprotection in macromolecular crystallography

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