Cryocrystallography of Biological Macromolecules

Schneider, T.

doi:10.12693/aphyspola.91.739

Cited by 2 publications

(2 citation statements)

References 23 publications

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“…However, the crystal cooling process typically leads to disruption of crystal order and, therefore, results in a decrease in diffraction quality. To overcome this problem, crystals are often soaked in a cryoprotective solution prior to cooling (Garman, 1999(Garman, , 2003Garman & Doublie, 2003;Garman & Owen, 2006;Haas & Rossmann, 1970;Henderson, 1990;Hope, 1988;Juers & Matthews, 2004;Kriminski et al, 2002;Rodgers, 1994;Schneider, 1997;Alcorn & Juers, 2010;Bujacz et al, 2010;Chinte et al, 2005;Garman & Mitchell, 1996;Mueller-Dieckmann et al, 2011;Petsko, 1975;Pflugrath, 2004;Rodgers, 1997;Warkentin et al, 2006). However, finding the optimal cryoprotective conditions for a given crystal often requires substantial time-consuming screening.…”

Section: Introductionmentioning

confidence: 99%

A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter

et al. 2012

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High-pressure cryocooling has been developed as an alternative method for cryopreservation of macromolecular crystals and successfully applied for various technical and scientific studies. The method requires the preservation of crystal hydration as the crystal is pressurized with dry helium gas. Previously, crystal hydration was maintained either by coating crystals with a mineral oil or by enclosing crystals in a capillary which was filled with crystallization mother liquor. These methods are not well suited to weakly diffracting crystals because of the relatively high background scattering from the hydrating materials. Here, an alternative method of crystal hydration, called capillary shielding, is described. The specimen is kept hydrated via vapor diffusion in a shielding capillary while it is being pressure cryocooled. After cryocooling, the shielding capillary is removed to reduce background X-ray scattering. It is shown that, compared to previous crystal-hydration methods, the new hydration method produces superior crystal diffraction with little sign of crystal damage. Using the new method, a weakly diffracting protein crystal may be properly pressure cryocooled with little or no addition of external cryoprotectants, and significantly reduced background scattering can be observed from the resulting sample. Beyond the applications for macromolecular crystallography, it is shown that the method has great potential for the preparation of noncrystalline hydrated biological samples for coherent diffraction imaging with future X-ray sources.

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Section: Introductionmentioning

confidence: 99%

A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter

et al. 2012

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“…However, it is common for the cooling process to disrupt the crystal order and decrease the diffraction quality. To address this problem, the crystal is often treated with a cryoprotective solution prior to cooling (Haas & Rossmann, 1970;Hope, 1988;Henderson, 1990;Rodgers, 1994;Garman & Schneider, 1997;Schneider, 1997;Garman, 1999Garman, , 2003Kriminski et al, 2002;Juers & Matthews, 2004b;Garman & Owen, 2006). Finding the optimal cryoprotective conditions is largely dependent on the crystal system and often involves substantial screening.…”

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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Cryocrystallography of Biological Macromolecules

Cited by 2 publications

References 23 publications

A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter

A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter

Progress in rational methods of cryoprotection in macromolecular crystallography

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