Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.7
Classification:PHOTOSYNTHESIS
Release Date:2001-09-05
Deposition Date:2001-06-27
Revision Date:2008-04-27#2011-07-13
Molecular Weight:102153.85
Macromolecule Type:Protein
Residue Count:848
Atom Site Count:6997
DOI:10.2210/pdb1jgz/pdb
Abstract:
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.
Resolution:2.7
Classification:PHOTOSYNTHESIS
Release Date:2001-09-05
Deposition Date:2001-06-27
Revision Date:2008-04-27#2011-07-13
Molecular Weight:102153.85
Macromolecule Type:Protein
Residue Count:848
Atom Site Count:6997
DOI:10.2210/pdb1jgz/pdb
Abstract:
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.
| Date made available | 2001 |
|---|---|
| Publisher | RCSB-PDB |