1jh0

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Photosynthetic Reaction Center Mutant With Glu L 205 Replaced to Leu

File:1jh0.gif


1jh0, resolution 3.50Å

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OverviewOverview

The role of contact interactions in the crystallization of membrane, proteins was assessed by mutation of amino-acid residues on the surface of, the reaction center from Rhodobacter sphaeroides. Five single-site mutants, were constructed, with changes in contact regions found in the trigonal, and tetragonal forms but not the orthorhombic form. Crystallization trials, for the tetragonal form yielded either no crystals or crystals with an, altered morphology, whereas crystals grew in the other two forms, indicating that these interactions are essential for the stability of the, tetragonal crystals. Changes in the structures determined by X-ray, diffraction of trigonal crystals for each mutant were related to the, quality of the diffraction. Significant differences in the resolution, limit of the crystals were associated with the loss of specific, interactions between neighboring proteins. The results suggest that the, contact regions are crucial for obtaining highly ordered crystals of, membrane proteins.

About this StructureAbout this Structure

1JH0 is a Protein complex structure of sequences from Rhodobacter sphaeroides with FE, BCL, BPH, U10 and SPO as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Individual interactions influence the crystalline order for membrane proteins., Camara-Artigas A, Magee CL, Williams JC, Allen JP, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1281-6. Epub 2001, Aug 23. PMID:11526320

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