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  Two-dimensional crystallization of human vitamin K-dependent γ-glutamyl carboxylase.

Schmidt-Krey, I., Haase, W., Mutucumarana, V., Stafford, D. W., & Kühlbrandt, W. (2007). Two-dimensional crystallization of human vitamin K-dependent γ-glutamyl carboxylase. Journal of Structural Biology, 157(2), 437-442. doi:10.1016/j.jsb.2006.08.002.

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 Creators:
Schmidt-Krey, Ingeborg1, Author
Haase, Winfried2, Author           
Mutucumarana, Vasantha3, Author
Stafford, Darrel W.3, Author
Kühlbrandt, Werner2, Author                 
Affiliations:
1Georgia Institute of Technology, School of Biology, 310 Ferst Drive, Atlanta, GA 30332-0230, USA, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3The University of North Carolina at Chapel Hill, Department of Biology and Center for Thrombosis and Hemostasis, Chapel Hill, 27599-3280, USA, ou_persistent22              

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Free keywords: Human vitamin K-dependent γ-glutamyl carboxylase; Two-dimensional crystallization; Electron crystallography; Blood coagulation; Anti-coagulation
 Abstract: Planar-tubular two-dimensional (2D) crystals of human vitamin K-dependent γ-glutamyl carboxylase grow in the presence of dimyristoyl phosphatidylcholine (DMPC). Surprisingly, these crystals form below the phase transition temperature of DMPC and at the unusually low molar lipid-to-protein (LPR) ratio of 1, while 2D crystals are conventionally grown above the phase transition temperature of the reconstituting lipid and significantly higher LPRs. The crystals are up to 0.75 μm in the shorter dimension of the planar tubes and at least 1 μm in length. Due to the planar-tubular nature of the crystals, two lattices are present. These are rotated by nearly 90° in respect to each other. The ordered arrays exhibit p121 plane group symmetry with unit cell dimensions of a = 83.7 Å, b = 76.6 Å, γ = 91°. Projection maps calculated from images of negatively stained and electron cryo-microscopy samples reveal the human vitamin K-dependent γ-glutamyl carboxylase to be a monomer.

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Language(s): eng - English
 Dates: 2006-08-082006-06-152006-08-082006-08-152007-02
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jsb.2006.08.002
PMID: 16979907
 Degree: -

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Title: Journal of Structural Biology
  Abbreviation : J. Struct. Biol.
Source Genre: Journal
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Publ. Info: San Diego, CA : Elsevier
Pages: - Volume / Issue: 157 (2) Sequence Number: - Start / End Page: 437 - 442 Identifier: ISSN: 1047-8477
CoNE: https://pure.mpg.de/cone/journals/resource/954922650160