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  Crystallization of proteinase K complexed with substrate analogue peptides on US space missions STS-91 and STS-95

Eschenburg, S., Degenhardt, M., Moore, K., DeLucas, L. J., Peters, K., Fittkau, S., et al. (2000). Crystallization of proteinase K complexed with substrate analogue peptides on US space missions STS-91 and STS-95. Journal of Crystal Growth, 208(1-4), 657-664. doi:10.1016/S0022-0248(99)00392-9.

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Genre: Journal Article
Alternative Title : Crystallization of proteinase K complexed with substrate analogue peptides on US space missions STS-91 and STS-95

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JCrystGrowth_208_2000_657.pdf (Any fulltext), 119KB
 
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 Creators:
Eschenburg, Susanne1, Author              
Degenhardt, Michael, Author
Moore, Karen, Author
DeLucas, Lawrence J., Author
Peters, Klaus, Author
Fittkau, Siegfried, Author
Weber, Wolfgang, Author
Betzel, Christian, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: Protein crystallization; Microgravity; X-ray crystallography
 Abstract: Crystals of proteinase K in complex with synthetic substrate analogues have been grown under microgravity on the US space shuttle missions STS-91 and STS-95 using the vapor diffusion apparatus (c-VDA) supplied by the Center for Macromolecular Crystallography at the University of Alabama at Birmingham. The crystals obtained under microgravity are compared with those grown simultanously on ground in identical c-VDA reactors and in conventional hanging-drop set-ups. The diffraction quality of space- and ground-grown crystals has been assessed by collecting complete data sets with a conventional X-ray source and with synchrotron radiation. Crystals grown in microgravity are clearly superior to those grown in the identical hardware on earth in terms of crystal habit and diffraction power. In comparison to best terrestrial crystals obtained in conventional hanging-drop set-ups the differences in crystal size and diffraction quality are less, but still confirm the benefit of microgravity for the crystallization of proteinase K–substrate analogue complexes.

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Language(s): eng - English
 Dates: 1998-06-241999-07-131999-12-202000-01-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Crystal Growth
Source Genre: Journal
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Publ. Info: Amsterdam : North-Holland
Pages: - Volume / Issue: 208 (1-4) Sequence Number: - Start / End Page: 657 - 664 Identifier: ISSN: 0022-0248
CoNE: https://pure.mpg.de/cone/journals/resource/954925412860