Production and crystallization of the C-propeptide trimer from human procollagen III

The C‐propeptide domains of the fibrillar procollagens, which are present throughout the Metazoa in the form of ∼90 kDa trimers, play crucial roles in both intracellular molecular assembly and extracellular formation of collagen fibrils. The first crystallization of a C‐propeptide domain, that from...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-10, Vol.68 (10), p.1209-1213
Main Authors: Bourhis, J.-M., Mariano, N., Zhao, Y., Walter, T. S., El Omari, K., Delolme, F., Moali, C., Hulmes, D. J. S., Aghajari, N.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Assembly
C-propeptide domain
Collagens
Crystallization
Crystallization Communications
Derivatives
Diffraction
HEK293 Cells
Human
Humans
Life Sciences
Mass spectrometry
Molecular Sequence Data
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Procollagen - chemistry
Procollagen - metabolism
procollagen III
Protein Multimerization
Selenomethionine
Trimers
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Summary:The C‐propeptide domains of the fibrillar procollagens, which are present throughout the Metazoa in the form of ∼90 kDa trimers, play crucial roles in both intracellular molecular assembly and extracellular formation of collagen fibrils. The first crystallization of a C‐propeptide domain, that from human procollagen III, is described. Following transient expression in mammalian 293T cells of both the native protein and a selenomethionine derivative, two crystal forms of the homotrimer were obtained: an orthorhombic form (P212121) that diffracted to 1.7 Å resolution and a trigonal form (P321) that diffracted to 3.5 Å resolution. Characterization by MALDI‐TOF mass spectrometry allowed the efficiency of selenomethionine incorporation to be determined.
ISSN:1744-3091
1744-3091
2053-230X
DOI:10.1107/S1744309112035294