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1crn

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WATER STRUCTURE OF A HYDROPHOBIC PROTEIN AT ATOMIC RESOLUTION. PENTAGON RINGS OF WATER MOLECULES IN CRYSTALS OF CRAMBIN

Overview

The water structure has been analyzed for a model of the protein crambin, refined against 0.945-A x-ray diffraction data. Crystals contain 32%, solvent by volume, and 77% of the solvent molecules have been, located-i.e., 2 ethanol molecules and 64 water molecules with 10-14, alternate positions. Many water oxygen atoms found form chains between, polar groups on the surface of the protein. However, a cluster of, pentagonal arrays made up of 16 water molecules sits at a hydrophobic, intermolecular cleft and forms a cap around the methyl group of, leucine-18. Several waters in the cluster are hydrogen-bonded directly to, the protein. Additional closed circular arrays, which include both protein, atoms and other water oxygen atoms, form next to the central cluster. This, water array stretches in the b lattice direction between groups of three, ionic side chains.

About this Structure

1CRN is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA.

Reference

Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin., Teeter MM, Proc Natl Acad Sci U S A. 1984 Oct;81(19):6014-6018. PMID:16593516

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