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

Eschenburg, Susanne; Degenhardt, Michael; Moore, Karen; DeLucas, Lawrence J.; Peters, Klaus; Fittkau, Siegfried; Weber, Wolfgang; Betzel, Christian

doi:10.1016/S0022-0248(99)00392-9

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

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Eschenburg, Susanne
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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http://dx.doi.org/10.1016/S0022-0248(99)00392-9
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Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0027-D13A-A

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.