Literature DB >> 12646373

Some notes on crystallizing fibrinogen and fibrin fragments.

Russell F Doolittle1.   

Abstract

We have recently determined the structure of a native fibrinogen at 2.7-A resolution. Not the least of the hurdles during the many years of this project was growing X-ray-grade crystals from suitably purified proteins. Small, synthetic peptides based on the parts of fibrinogen exposed by the action of thrombin contributed greatly to these experiments. In addition, trimethylamine oxide (TMAO) was found to improve the diffraction of fibrinogen crystals. The history of my interest in fibrinogen and its crystallization can be traced back in part to some early interactions with John Edsall.

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Year:  2003        PMID: 12646373     DOI: 10.1016/s0301-4622(02)00288-0

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  2 in total

1.  Crystallization of a functionally intact Hsc70 chaperone.

Authors:  Jianwen Jiang; Eileen M Lafer; Rui Sousa
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-12-16

2.  Volume exclusion and H-bonding dominate the thermodynamics and solvation of trimethylamine-N-oxide in aqueous urea.

Authors:  Jörg Rösgen; Ruby Jackson-Atogi
Journal:  J Am Chem Soc       Date:  2012-02-10       Impact factor: 15.419

  2 in total

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