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  Production, crystallization, and preliminary X-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1-47) of troponin I

Saijo, Y., Takeda, S., Scherer, A., Kobayashi, T., Maéda, Y., Taniguchi, H., et al. (1997). Production, crystallization, and preliminary X-ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1-47) of troponin I. Protein Science, 6(4), 916-918. doi:10.1002/pro.5560060420.

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ProtSci_6_1997_916.pdf (Any fulltext), 321KB
 
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 Creators:
Saijo, Yumiko, Author
Takeda, Soichi, Author
Scherer, Anna1, Author              
Kobayashi, T.2, Author              
Maéda, Yuichiro, Author
Taniguchi, Hisaaki, Author
Yao, Min, Author
Wakatsuki, Soichi, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: chemical cleavage; crystallization; mass spectrometry; skeletal muscle regulation; troponin; X-ray crystallography
 Abstract: Troponin is a ternary protein complex consisting of subunits TnC. TnI, and TnT, and plays a key role in calcium regulation of the skeletal and cardiac muscle contraction. In the present study, a partial complex (CI47) was prepared from Escherichia coli-expressed rabbit skeletal muscle TnC and fragment 1-47 of TnI, which is obtained by chemical cleavage of an E. coli-expressed mutant of rabbit skeletal muscle TnI. Within the ternary troponin complex, CI47 is thought to form a core that is resistant to proteolytic digestion, and the interaction within CI47 likely maintains the integrity of the troponin complex. Complex CI47 was crystallized in the presence of sodium citrate. The addition of trehalose improved the diffraction pattern of the crystals substantially. The crystal lattice belongs to the space group P3(1)(2)21, with unit cell dimensions a = b = 48.2 A, c = 162 A. The asymmetric unit presumably contains one CI47 complex. Soaking with p-chloromercuribenzenesulfonate (PCMBS) resulted in loss of isomorphism, but enhanced the quality of the crystals. The crystals diffracted up to 2.3 A resolution, with completeness of 91% and R(merge) = 6.4%. The crystals of PCMBS-derivative should be suitable for X-ray studies using the multiple-wavelength anomalous diffraction technique. This is the first step for elucidating the structure of the full troponin complex.

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Language(s): eng - English
 Dates: 1996-06-241997-01-132008-12-311997-04
 Publication Status: Published in print
 Pages: 3
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 Table of Contents: -
 Rev. Type: Peer
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Title: Protein Science
Source Genre: Journal
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Publ. Info: New York, N.Y. : Cambridge University Press
Pages: - Volume / Issue: 6 (4) Sequence Number: - Start / End Page: 916 - 918 Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760