Protein crystal growth in microgravity

Lawrence J. DeLucas; Craig D. Smith; H. Wilson Smith; Senadhi Vijay-Kumar; Shobha E. Senadhi; Steven E. Ealick; Daniel C. Carter; Robert S. Snyder; Patricia C. Weber; F. Raymond Salemme; D. H. Ohlendorf; H. M. Einspahr; L. L. Clancy; Manuel A. Navia; Brian M. McKeever; T. L. Nagabhushan; George Nelson; A. Mcpherson; S. Koszelak; G. Taylor; D. Stammers; K. Powell; G. Darby; Charles E. Bugg

doi:10.1126/science.2510297

Protein crystal growth in microgravity

Lawrence J. DeLucas, Craig D. Smith, H. Wilson Smith, Senadhi Vijay-Kumar, Shobha E. Senadhi, Steven E. Ealick, Daniel C. Carter, Robert S. Snyder, Patricia C. Weber, F. Raymond Salemme, D. H. Ohlendorf, H. M. Einspahr, L. L. Clancy, Manuel A. Navia, Brian M. McKeever, T. L. Nagabhushan, George Nelson, A. Mcpherson, S. Koszelak, G. TaylorD. Stammers, K. Powell, G. Darby, Charles E. Bugg

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

163 Scopus citations

Abstract

The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of γ-interferon D ¹, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.

Original language	English (US)
Pages (from-to)	651-654
Number of pages	4
Journal	Science
Volume	246
Issue number	4930
DOIs	https://doi.org/10.1126/science.2510297
State	Published - 1989

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DeLucas, L. J., Smith, C. D., Smith, H. W., Vijay-Kumar, S., Senadhi, S. E., Ealick, S. E., Carter, D. C., Snyder, R. S., Weber, P. C., Salemme, F. R., Ohlendorf, D. H., Einspahr, H. M., Clancy, L. L., Navia, M. A., McKeever, B. M., Nagabhushan, T. L., Nelson, G., Mcpherson, A., Koszelak, S., ... Bugg, C. E. (1989). Protein crystal growth in microgravity. Science, 246(4930), 651-654. https://doi.org/10.1126/science.2510297

DeLucas, LJ, Smith, CD, Smith, HW, Vijay-Kumar, S, Senadhi, SE, Ealick, SE, Carter, DC, Snyder, RS, Weber, PC, Salemme, FR, Ohlendorf, DH, Einspahr, HM, Clancy, LL, Navia, MA, McKeever, BM, Nagabhushan, TL, Nelson, G, Mcpherson, A, Koszelak, S, Taylor, G, Stammers, D, Powell, K, Darby, G & Bugg, CE 1989, 'Protein crystal growth in microgravity', Science, vol. 246, no. 4930, pp. 651-654. https://doi.org/10.1126/science.2510297

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title = "Protein crystal growth in microgravity",

abstract = "The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of γ-interferon D 1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.",

author = "DeLucas, {Lawrence J.} and Smith, {Craig D.} and Smith, {H. Wilson} and Senadhi Vijay-Kumar and Senadhi, {Shobha E.} and Ealick, {Steven E.} and Carter, {Daniel C.} and Snyder, {Robert S.} and Weber, {Patricia C.} and Salemme, {F. Raymond} and Ohlendorf, {D. H.} and Einspahr, {H. M.} and Clancy, {L. L.} and Navia, {Manuel A.} and McKeever, {Brian M.} and Nagabhushan, {T. L.} and George Nelson and A. Mcpherson and S. Koszelak and G. Taylor and D. Stammers and K. Powell and G. Darby and Bugg, {Charles E.}",

year = "1989",

doi = "10.1126/science.2510297",

language = "English (US)",

volume = "246",

pages = "651--654",

journal = "Science",

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T1 - Protein crystal growth in microgravity

AU - DeLucas, Lawrence J.

AU - Smith, Craig D.

AU - Smith, H. Wilson

AU - Vijay-Kumar, Senadhi

AU - Senadhi, Shobha E.

AU - Ealick, Steven E.

AU - Carter, Daniel C.

AU - Snyder, Robert S.

AU - Weber, Patricia C.

AU - Salemme, F. Raymond

AU - Ohlendorf, D. H.

AU - Einspahr, H. M.

AU - Clancy, L. L.

AU - Navia, Manuel A.

AU - McKeever, Brian M.

AU - Nagabhushan, T. L.

AU - Nelson, George

AU - Mcpherson, A.

AU - Koszelak, S.

AU - Taylor, G.

AU - Stammers, D.

AU - Powell, K.

AU - Darby, G.

AU - Bugg, Charles E.

PY - 1989

Y1 - 1989

N2 - The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of γ-interferon D 1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.

AB - The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of simple organic and inorganic compounds. Crystallization in the microgravity environment of space may improve crystal quality by eliminating convection effects near growing crystal surfaces. A series of 11 different protein crystal growth experiments was performed on U.S. space shuttle flight STS-26 in September 1988. The microgravity-grown crystals of γ-interferon D 1, porcine elastase, and isocitrate lyase are larger, display more uniform morphologies, and yield diffraction data to significantly higher resolutions than the best crystals of these proteins grown on Earth.

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SN - 0036-8075

VL - 246

SP - 651

EP - 654

JO - Science

JF - Science

IS - 4930

ER -

Protein crystal growth in microgravity

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