Control of nucleation in the crystallization of lysozyme

Chayen, Naomi E.; Radcliffe, Jonathan; Blow, D. M.

doi:10.1002/pro.5560020112

Cited by 48 publications

(36 citation statements)

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“…Some reports also propose that the effects of the protein previous thermal history and the storage time of a protein solution are potentially critical factors in macromolecule crystal nucleation. [15][16][17] In conclusion, we tried to grow HEWL crystals using the slow-cooling method instead of the vapor-diffusion method. The number and size of crystals obtained were greatly dependent on the cooling rate up to spontaneous nucleation.…”

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Effective Protein Crystallization Using Crystal Hysteresis

Adachi

Takano

Yoshimura

et al. 2003

Jpn. J. Appl. Phys.

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We have developed a new method for protein crystallization, crystal hysteresis, that utilizes slow-cooling and recooling techniques. Slow cooling of a saturated solution enables precise control of supersaturation in the solution and also allows reuse of the solution because it maintains its composition. Examination of the effects of various cooling rates on hen egg-white lysozyme crystallization revealed that the cooling rate determined the number and size of the obtained crystals. Furthermore, recrystallization of lysozyme from the same solution after dissolving the previously grown crystals was found to be very effective in reducing the number of nucleation sites, thus obtaining larger crystals.

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confidence: 99%

Effective Protein Crystallization Using Crystal Hysteresis

Adachi

Takano

Yoshimura

et al. 2003

Jpn. J. Appl. Phys.

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“…This makes the microbatch an ideal environment for controlled heterogeneous nucleation experiments (Chayen, Radcliffe & Blow, 1993;Blow, Chayen, Lloyd & Saridakis, 1994;Chayen, 1996). Heterogeneous nucleation, which is often detrimental to the production of suitable crystals for X-ray diffraction, can be induced by the contact of a crystallization sample with the walls of its supporting vessel (Yonath, M/issig & Wittmann, 1982).…”

Section: Comparison Of the Vapour-diffusion And Microbatch Methodsmentioning

confidence: 99%

Comparative Studies of Protein Crystallization by Vapour-Diffusion and Microbatch Techniques

Chayen

1998

Acta Crystallogr D Biol Crystallogr

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104

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IntroductionNumerous reports have been published in the literature which describe the crystallization of macromolecules by a variety of crystallization methods, including the vapour-diffusion and microbatch techniques. This topical review compares the results of examples of proteins which were crystallized by both vapour-diffusion and microbatch methods. The inherent features of the vapourdiffusion and microbatch methods are discussed and some specific conditions where one method appears more favourable than the other are reported. Guidelines for the conversion of crystallization conditions from vapour diffusion to microbatch (and vice versa) are also presented.

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“…There have been several substances that have been tried more or less successful. Some have been useful for individual proteins, but mostly they were not applicable in general (McPherson and Shlichta 1988;Chayen, Radcliffe et al 1993;Blow, Chayen et al 1994 proposed the idea of using porous silicon whose pore size is comparable with the size of a protein molecule. In theory such pores may confine and concentrate the protein molecules at the surface of the silicone and thereby encourage them to form crystal nuclei (Chayen, Saridakis et al 2001).…”

Section: Crystal Nucleationmentioning

confidence: 99%