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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2012
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309112035294
- pmid
- 23027749
- Publisher site
- See Article on Publisher Site
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 (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.
Journal
Acta Crystallographica Section F – Wiley
Published: Oct 1, 2012