DOI: 10.1002/pro.5560050426. High level expression and crystallization of recombinant human cathepsin S

High level expression and crystallization of recombinant human cathepsin S

10.1002/pro.5560050426

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractWe have expressed active human cathepsin S to 60 mg/L in Sf9 cells using a baculovirus system. Production of milligram quantities has facilitated crystallographic studies to determine the structure of this enzyme, which has unique properties among lysosomal cysteine proteinases. Recombinant, irreversibly inhibited cathepsin S was crystallized from ammonium phosphate at 17 °C. The crystals diffract to at least 2.3 Å, and belong to the orthorhombic crystal system with a primitive lattice. Approximate cell dimensions are: a = 37.7 Å, b = 73.9 Å, and c = 106.7 Å. There is most likely one molecule per asymmetric unit.

Bibliography

BrÃ¶mme, D., & Mcgrath, M. E. (1996). High level expression and crystallization of recombinant human cathepsin S. Protein Science, 5(4), 789â791. Portico.

Authors 2

Dieter Brömme (first)
Mary E. Mcgrath (additional)

References 27 Referenced 35

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10.1038/314194a0

Dates

Type	When
Created	15 years, 1 month ago (July 12, 2010, 4:18 a.m.)
Deposited	1 year, 10 months ago (Oct. 26, 2023, 4:54 p.m.)
Indexed	1 year, 9 months ago (Nov. 23, 2023, 8:37 a.m.)
Issued	29 years, 5 months ago (April 1, 1996)
Published	29 years, 5 months ago (April 1, 1996)
Published Online	16 years, 8 months ago (Dec. 31, 2008)
Published Print	29 years, 5 months ago (April 1, 1996)

Funders 0

None

BibTeX

@article{Br_mme_1996, title={High level expression and crystallization of recombinant human cathepsin S}, volume={5}, ISSN={1469-896X}, url={http://dx.doi.org/10.1002/pro.5560050426}, DOI={10.1002/pro.5560050426}, number={4}, journal={Protein Science}, publisher={Wiley}, author={Brömme, Dieter and Mcgrath, Mary E.}, year={1996}, month=apr, pages={789–791} }

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