1ctf: Difference between revisions

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==Overview==

The structure of a C-terminal fragment of the ribosomal protein L7/L12, from Escherichia coli has been refined using crystallographic data to 1.7, A resolution. The R-value is 17.4%. Six residues at the N terminus are too, disordered in the structure to be localized. These residues are probably, part of a hinge in the complete L7/L12 molecule. The possibility that a, 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A, patch of invariant residues on the surface of the dimer is probably, involved in functional interactions with elongation factors.

The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.

==About this Structure==

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[[Category: ribosomal protein]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The structure of a C-terminal fragment of the ribosomal protein L7/L12, from Escherichia coli has been refined using crystallographic data to 1.7, A resolution. The R-value is 17.4%. Six residues at the N terminus are too, disordered in the structure to be localized. These residues are probably, part of a hinge in the complete L7/L12 molecule. The possibility that a, 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A, patch of invariant residues on the surface of the dimer is probably, involved in functional interactions with elongation factors.
+The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.
 ==About this Structure==
@@ Line 18: / Line 18: @@
 [[Category: ribosomal protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:37:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:36 2008''