Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by BROMME, D.
Right arrow Articles by MCGRATH, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by BROMME, D.
Right arrow Articles by MCGRATH, M. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 5, Issue 4 789-791, Copyright © 1996 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

High level expression and crystallization of recombinant human cathepsin S

D. BROMME and M. E. MCGRATH
Khepri Pharmaceuticals, Inc., South San Francisco, California 94080

We 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{deg}C. The crystals diffract to at least 2.3 A, and belong to the orthorhombic crystal system with a primitive lattice. Approximate cell dimensions are: a = 37.7 A, b = 73.9 A, and c = 106.7 A. There is most likely one molecule per asymmetric unit.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Y. Choe, F. Leonetti, D. C. Greenbaum, F. Lecaille, M. Bogyo, D. Bromme, J. A. Ellman, and C. S. Craik
Substrate Profiling of Cysteine Proteases Using a Combinatorial Peptide Library Identifies Functionally Unique Specificities
J. Biol. Chem., May 5, 2006; 281(18): 12824 - 12832.
[Abstract] [Full Text] [PDF]

Home page
 JEMHome page
G.-P. Shi, R. A.R. Bryant, R. Riese, S. Verhelst, C. Driessen, Z. Li, D. Bromme, H. L. Ploegh, and H. A. Chapman
Role for Cathepsin F in Invariant Chain Processing and Major Histocompatibility Complex Class II Peptide Loading by Macrophages
J. Exp. Med., April 3, 2000; 191(7): 1177 - 1186.
[Abstract] [Full Text] [PDF]

Home page
 JEMHome page
J. A. Villadangos, R. J. Riese, C. Peters, H. A. Chapman, and H. L. Ploegh
Degradation of Mouse Invariant Chain: Roles of Cathepsins S and D and the Influence of Major Histocompatibility Complex Polymorphism
J. Exp. Med., August 18, 1997; 186(4): 549 - 560.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Stoka, B. Turk, S. L. Schendel, T.-H. Kim, T. Cirman, S. J. Snipas, L. M. Ellerby, D. Bredesen, H. Freeze, M. Abrahamson, et al.
Lysosomal Protease Pathways to Apoptosis. CLEAVAGE OF Bid, NOT PRO-CASPASES, IS THE MOST LIKELY ROUTE
J. Biol. Chem., January 26, 2001; 276(5): 3149 - 3157.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by The Protein Society.