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Journal Article

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

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Haase,  Winfried
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D8A3-F
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.