Parameters for crystal growth of ribosomal subunits

Yonath, Ada; Müssig, J.; Wittmann, H. G.

doi:10.1002/jcb.240190205

Cited by 65 publications

(24 citation statements)

References 14 publications

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“…The most likely is the lack of contact of the crystallization drop with the surface of the well. It has been reported that contact between the two is known to increase heterogeneous nucleation which commonly gives rise to large numbers of poorly formed crystals 11 . The shape of the crystallization drop has also been shown to be an influencing factor in crystallization experiments.…”

Section: Resultsmentioning

confidence: 99%

Upside‐Down Protein Crystallization

Khurshid

Chayen

2006

Annals of the New York Academy of Sciences

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The benefits of protein crystal growth in microgravity are well documented. The crystallization vessels currently employed for microgravity crystallization are far from optimal with regards to cost, sample volume, size, and ease of use. The use of microbatch experiments is a favorable alternative in each respect: 96 experiments of 0.5-2 microL volumes can be performed in a single microtiter tray measuring 5 x 8 cm and costing 1 pound sterling each. To date, the use of microbatch has not been pursued on account of concerns of oil leakage. To address this issue, a novel approach to microbatch crystallization experiments is described, where the microbatch plates are inverted throughout the duration of the experiment. The findings intimate the application of the microbatch method to space flight and the potential to drastically increase the output of microgravity crystallization research .

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Section: Resultsmentioning

confidence: 99%

Upside‐Down Protein Crystallization

Khurshid

Chayen

2006

Annals of the New York Academy of Sciences

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“…Komatsu, Miyashita & Suzuki, 1993). Enlargement of drops in vapour-diffusion trials can be prevented or reversed by the addition of salt to the reservoir as described by Yonath, Mfissig & 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

105

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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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“…The crystals were grown employing a slightly modified version of the vapour diffusion technique in hanging drops, depression slides and in capillaries [9,13]. The crystallization drops which contained the ribosomes and MES, HEPES or glycine buffers (pH 6.0-9.0) were equilibrated with organic solvents (see below) in the presence of 0.5-0.9 M NaC1 and 6 mM fl-mercaptoethanol in the reservoir, at 3-7°C.…”

Section: Crystallizationmentioning

confidence: 99%

“…The first three-dimensional crystals of ribosomal particles were obtained in vitro from the large subunit of the Bacillus stearothermophilus ribosome [8,9]. These have been characterized by three-dimensional image reconstruction studies [10].…”

Section: Introductionmentioning

confidence: 99%