Crystallization of proteins under microgravity

Erdmann, Volker A.; Lippmann, Corinna; Betzel, Christian; Dauter, Z.; Wilson, Keith; Hilgenfeld, Rolf; Hoven, Julia; Liesum, A.; Müller‐Fahrnow, Anke; Hinrichs, W.; Düvel, Martina; Schulz, Georg E.; Müller, Christoph; Wittmann, H. G.; Yonath, Ada; Weber, G.; Stegen, Karin; Plaas-Link, Andreas

doi:10.1016/0014-5793(89)81526-1

Cited by 35 publications

(16 citation statements)

References 9 publications

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“…It is fair to say that not all microgravity experiments share the same conclusion (Erdmann et al, 1989;Hilgenfeld, Liesum, Storm & Plaas-Link, 1992;Stoddard, Strong, Arrott & Farber, 1992). For example, it could be shown for crystals grown during the unmanned COSIMA-2 mission that spacegrown crystals of Streptomyces coelicolor lysozyme and Bacillus thermoproteolyticus were of worse quality than the ground controls (Hilgenfeld et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Thaumatin Crystals Grown on Earth and in Microgravity

Lorber²,

Giegé³

et al. 1997

Acta Cryst D

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The protein thaumatin was studied as a model macromolecule for crystallization in microgravity-environment experiments conducted on two US Space Shuttle missions (USML-2 and LMS). In this investigation, we have evaluated and compared the quality of space-and earth-grown thaumatin crystals using X-ray diffraction analyses, and characterized them according to crystal size, diffraction resolution limit and mosaicity. Two different approaches for growing thaumatin crystals in the microgravity environment, dialysis and liquid-liquid diffusion, were employed as a joint experiment by our two investigative teams. Thaumatin crystals grown in a microgravity environment were generally larger in volume and the total number of crystals was less, relative to crystals grown on earth. They diffracted to significantly higher resolution and with improved diffraction (/,,)

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Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Thaumatin Crystals Grown on Earth and in Microgravity

Lorber²,

Giegé³

et al. 1997

Acta Cryst D

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“…Evidence has accumulated over the past several years, from a variety of experiments carried out in microgravity, that protein crystals of improved qualities or increased order can be grown under reduced gravity conditions (Littke andJohn, 1984,1986;Littke, 1985Littke, , 1988DeLucas et al, 1986DeLucas et al, , 1989DeLucas et al, , 1991aDeLucas & Bugg, 1987;Giege et al, 1988;Erdmann et al, 1989;McPherson et al, 1991).…”

mentioning

confidence: 99%

Macromolecular crystal growth experiments on international microgravity laboratory – 1

Day

McPherson

1992

Protein Science

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Macromolecular crystal growth experiments, using satellite tobacco mosaic virus (STMV) and canavalin from jack beans as samples, were conducted on a US Space Shuttle mission designated International Microgravity Laboratory-1 (IML-I), flown January [22][23][24][25][26][27][28][29] 1992. Parallel experiments using identical samples were carried out in both a vapor diffusion-based device (PCG) and a liquid-liquid diffusion-based instrument (CRYOSTAT). The experiments in each device were run at 20-22 "C and at colder temperatures.Crystals were grown in virtually every trial, but the characteristics of the crystals were highly dependent on the crystallization technique employed and the temperature experience of the sample. In general, very good results, based on visual inspection of the crystals, were obtained in both PCG and CRYOSTAT. Unusually impressive results were, however, achieved for STMV in the CRYOSTAT instrument. STMV crystals grown in microgravity by liquid-liquid diffusion were more than IO-fold greater in total volume than any STMV crystals previously grown in the laboratory.X-ray diffraction data collected from eight STMV crystals grown in CRYOSTAT demonstrated a substantial improvement in diffraction quality over the entire resolution range when compared to data from crystals grown on Earth. In addition, the extent of the diffraction pattern for the STMV crystals grown in space extended to 1.8 A resolution, whereas the best crystals that were ever grown under conditions of Earth's gravity produced data limited to 2.3 A resolution.Other observations indicate that the growth of macromolecular crystals is indeed influenced by the presence or absence of gravity. These observations further suggest, consistent with earlier results, that the elimination of gravity provides a more favorable environment for such processes.

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“…39 According to the results of calculations, 10 76 g (microgravity) is sufficient to suppress the influence of convection, i.e., for the diffusive mass transport to dominate. 28 Microgravity conditions can be achieved in outer space.…”

Section: Crystallization Methods Suppressing the Convective Mass mentioning

confidence: 99%

“…70 However, microgravity does not lead to a desired increase in the crystal quality of some proteins. 39 The crystallization in outer space is performed using such well-known methods as vapour diffusion, 71, 72 counterdiffusion 12, 73, 74 and dialysis. 75,76 The equipment for such experiments is modified (and sometimes specially designed) taking into account the specific features of outer-space experiments.…”

Section: Iv4 True Microgravitymentioning

confidence: 99%