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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biophysik     Display Documents



ID: 565667.0, MPI für medizinische Forschung / Abteilung Biophysik
Production, crystallization, and preliminary X−ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1−47) of troponin I
Translation of Title:Production, crystallization, and preliminary X−ray analysis of rabbit skeletal muscle troponin complex consisting of troponin C and fragment (1−47) of troponin I
Authors:Saijo, Y.; Takeda, S.; Scherer, Anna; Kobayashi, T.; Maeda, Y.; Taniguchi, T.; Yao, M.; Wakatsuki, S.
Language:English
Date of Publication (YYYY-MM-DD):1997-04-01
Title of Journal:Protein Science
Journal Abbrev.:Protein Science
Volume:6
Issue / Number:4
Start Page:916
End Page:918
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
Identifiers:LOCALID:5420
URI:http%3A%2F%2Fwww.proteinscience.org%2Fcgi%2Freprin...
URI:http%3A%2F%2Fwww.proteinscience.org%2Fcgi%2Fconten...
DOI:10.1002%2Fpro.5560060420
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