Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

Science

Volumn 271, Issue 5246, 1996, Pages 203-207

  Mande, Shekhar C ^a   Mehra, Vijay ^a   Bloom, Barry R ^a,b   Hol, Wim G J ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; HEAT SHOCK PROTEIN; OLIGOMER;

ARTICLE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; HYDROPHILICITY; MYCOBACTERIUM LEPRAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0030024540     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5246.203     Document Type: Article

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46. We thank the members of the Biomolecular Structure Center for support regarding synchrotron and computing aspects of these studies, in particular S. Turley, C. Verlinde, and E. Merritt. The assistance of I. Feil in site-directed mutagenesis studies is appreciated Access to the Stanford Synchrotron Radiation Laboratories is gratefully acknowledged. This work was supported by NIH grants A107118 and 23545, the Howard Hughes Medical Institute, the Immunology of Mycobacteria (IMMMYC) program of the United Nations Development Programme-World Bank-World Health Organization Special Program for Research and Training in Tropical Diseases, a major equipment grant from the Murdock Charitable Trust to the Biomolecular Structure Center, and by the School of Medicine of the University of Washington, Seattle, WA. The coordinates for M. Leprae cpn10 have been deposited with the Brookhaven Protein Data Bank.