Crystallization of bovine pancreatic polypeptide in the presence of crystalline diglycidyl ether of bisphenol A (Araldite): epitaxy or covalent nucleation?

Wood, Steve; Janes, Robert W.; Sweeney, Emma; Palmer, R. A.

doi:10.1016/0022-0248(92)90246-f

Cited by 6 publications

(4 citation statements)

References 7 publications

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“…It has also been applied to ensure greater reproducibility. There are now numerous reports in the literature of the use of mineral substrates (McPherson & Schlichta, 1989), polymeric surfaces such as epoxides (Wood et al, 1991), the keratin hairs of various animals (D'Arcy et al, 2003), including humans (Leung et al, 1989), graphoepitaxy (Saridakis et al, 2011;Givargizov, 2008) and epitaxy on specialized materials (Pum et al, 1993). The point that all of these experiences illustrate is that surfaces are important in crystallization, particularly at the nucleation stage.…”

Section: Surfacesmentioning

confidence: 99%

Optimization of crystallization conditions for biological macromolecules

McPherson

Cudney²

2014

Acta Crystallogr F Struct Biol Commun

107

112

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For the successful X-ray structure determination of macromolecules, it is first necessary to identify, usually by matrix screening, conditions that yield some sort of crystals. Initial crystals are frequently microcrystals or clusters, and often have unfavorable morphologies or yield poor diffraction intensities. It is therefore generally necessary to improve upon these initial conditions in order to obtain better crystals of sufficient quality for X-ray data collection. Even when the initial samples are suitable, often marginally, refinement of conditions is recommended in order to obtain the highest quality crystals that can be grown. The quality of an X-ray structure determination is directly correlated with the size and the perfection of the crystalline samples; thus, refinement of conditions should always be a primary component of crystal growth. The improvement process is referred to as optimization, and it entails sequential, incremental changes in the chemical parameters that influence crystallization, such as pH, ionic strength and precipitant concentration, as well as physical parameters such as temperature, sample volume and overall methodology. It also includes the application of some unique procedures and approaches, and the addition of novel components such as detergents, ligands or other small molecules that may enhance nucleation or crystal development. Here, an attempt is made to provide guidance on how optimization might best be applied to crystal-growth problems, and what parameters and factors might most profitably be explored to accelerate and achieve success.

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Section: Surfacesmentioning

confidence: 99%

Optimization of crystallization conditions for biological macromolecules

McPherson

Cudney²

2014

Acta Crystallogr F Struct Biol Commun

107

112

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“…Additional factors have emerged both from recent crystal growth research, and from the empirical results generated by the current revolution in crystallography. Among these factors are the importance of surfaces and their promotion of heterogeneous nucleation [79][80][81][82]; the value of unique environments such as microgravity [41][42][43]83], gels [84-86] and thin capillaries [87]; the broad range of polymeric precipitants found to be useful in growing crystals [88][89]; and new approaches to solving the problem of persistent microcrystals [90].…”

Section: Conditions For Macromolecular Crystal Growthmentioning

confidence: 99%

The science of macromolecular crystallization

1995

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For the X-ray crystallographer, the future of his field is, and has always been, determined by what he is able to crystallize. This is now particularly true as a result of the extraordinary improvement in X-ray detectors and sources [1], the advent of computers of amazing speed, and the development of programs that are both friendly and efficient [2]. The critical component, trailing other technology, is the growth of crystals of macromolecules having sufficient size and quality to permit X-ray analysis.Crystallization, however, has become less problematic. With synchrotron sources [3], sensitive, fast detectors, cryogenic techniques that eliminate radiation damage [4], and more powerful phasing tools, both the number and the size of crystals required for the analysis has decreased: crystals of 30-50 ,pm may soon be adequate, frozen crystals often provide a complete data set, and molecular replacement can allow determination of entire structures from this one set. Equally importantly, crystallization procedures, reagents, and diagnostic tools are now available that greatly improve the probability of success for both experienced crystallographers and interested biochemists.

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“…In homogeneous nucleation, crystal nuclei are spontaneously formed from the supersaturated protein aqueous solution, indicating spontaneous nucleation. In contrast, in heterogeneous nucleation, a different type of solid substance referred to as the 'nucleant' promotes nucleation, and this is thought to improve the crystallizability of proteins and to minimize the protein quantity required for crystallization (McPherson & Shlichta, 1988;Chayen et al, , 2006Edwards et al, 1994;Hemming et al, 1995;Ray & Bracker, 1986;Leung et al, 1989;Punzi et al, 1991;Wood et al, 1992;Falini et al, 2002). Whether nucleation is spontaneous or directed depends upon the type of nucleant used and how it is used.…”

Section: Introductionmentioning

confidence: 99%

Nucleant-mediated protein crystallization with the application of microporous synthetic zeolites

Sugahara

Asada

Morikawa

et al. 2008

Acta Crystallogr D Biol Crystallogr

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Protein crystallization is still a major bottleneck in structural biology. As the current methodology of protein crystallization is a type of screening, it is usually difficult to crystallize important target proteins. It was thought that hetero-epitaxic growth from the surface of a mineral crystal acting as a nucleant would be an effective enhancer of protein crystallization. However, in spite of almost two decades of effort, a generally applicable hetero-epitaxic nucleant for protein crystallization has yet to be found. Here we introduce the first candidate for a universal hetero-epitaxic nucleant, microporous zeolite: a synthetic aluminosilicate crystalline polymer with regular micropores. It promotes a form-selective crystal nucleation of proteins and acts as a crystallization catalyst. The most successful zeolite nucleant was molecular sieve type 5A with a pore size of 5 A and with bound Ca2+ ions. The zeolite-mediated crystallization improved the crystal quality in five out of six proteins tested. It provided new crystal forms with better resolution in two cases, larger crystals in one case, and zeolite-dependent crystal formations in two cases. The hetero-epitaxic growth of the zeolite-mediated crystals was confirmed by a crystal-packing analysis which revealed a layer-like structure in the crystal lattice.

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Crystallization of bovine pancreatic polypeptide in the presence of crystalline diglycidyl ether of bisphenol A (Araldite): epitaxy or covalent nucleation?

Cited by 6 publications

References 7 publications

Optimization of crystallization conditions for biological macromolecules

Optimization of crystallization conditions for biological macromolecules

The science of macromolecular crystallization

Nucleant-mediated protein crystallization with the application of microporous synthetic zeolites

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