title: Production and crystallization of the C-propeptide trimer from human procollagen III.
abstract: 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 (P2(1)2(1)2(1)) 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.
authors.affiliation: FRE 3310, Institut de Biologie et Chimie des Protéines, CNRS/Université Lyon 1, 69367 Lyon CEDEX 7, France.
authors.forename: J-M
authors.initials: JM
authors.lastname: Bourhis
authors.forename: N
authors.initials: N
authors.lastname: Mariano
authors.forename: Y
authors.initials: Y
authors.lastname: Zhao
authors.forename: T S
authors.initials: TS
authors.lastname: Walter
authors.forename: K
authors.initials: K
authors.lastname: El Omari
authors.forename: F
authors.initials: F
authors.lastname: Delolme
authors.forename: C
authors.initials: C
authors.lastname: Moali
authors.forename: D J S
authors.initials: DJ
authors.lastname: Hulmes
authors.forename: N
authors.initials: N
authors.lastname: Aghajari
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D057809:HEK293 Cells; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011347:Procollagen / Q000737:chemistry* / Q000378:metabolism; D055503:Protein Multimerization
chemical_list: D010446:Peptide Fragments; D011347:Procollagen