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.
| Original language | English |
|---|---|
| Pages (from-to) | 1281-1286 |
| Number of pages | 6 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 57 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 2001 |
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ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology
Cite this
Individual interactions influence the crystalline order for membrane proteins. / Camara-Artigas, A.; Magee, C. L.; Williams, J. C.; Allen, James Paul.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 9, 2001, p. 1281-1286.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Individual interactions influence the crystalline order for membrane proteins
AU - Camara-Artigas, A.
AU - Magee, C. L.
AU - Williams, J. C.
AU - Allen, James Paul
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
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U2 - 10.1107/S090744490101109X
DO - 10.1107/S090744490101109X
M3 - Article
C2 - 11526320
AN - SCOPUS:0034834616
VL - 57
SP - 1281
EP - 1286
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 9
ER -