1okh: Difference between revisions

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==Overview==

The crystal structure of viscotoxin A3 (VT A3) extracted from European, mistletoe (Viscum album L.) has been solved using the anomalous, diffraction of the native S atoms measured in-house with Cu Kalpha, radiation to a resolution of 2.2 A and truncated to 2.5 A. A 1.75 A, resolution synchrotron data set was used for phase expansion and, refinement. An innovation in the dual-space substructure-solution program, SHELXD enabled the individual S atoms of the disulfide bonds to be located, using the Cu Kalpha data; this resulted in a marked improvement in the, phasing compared with the use of super-S atoms. The VT A3 monomer consists, of 46 amino acids with three disulfide bridges and has an overall fold, resembling the canonical architecture of the alpha- and beta-thionins, a, capital letter L. The asymmetric unit consists of two monomers related by, a local twofold axis and held together by hydrophobic interactions between, the monomer units. One phosphate anion (confirmed by 31P-NMR and MS) is, associated with each monomer.

The crystal structure of viscotoxin A3 (VT A3) extracted from European mistletoe (Viscum album L.) has been solved using the anomalous diffraction of the native S atoms measured in-house with Cu Kalpha radiation to a resolution of 2.2 A and truncated to 2.5 A. A 1.75 A resolution synchrotron data set was used for phase expansion and refinement. An innovation in the dual-space substructure-solution program SHELXD enabled the individual S atoms of the disulfide bonds to be located using the Cu Kalpha data; this resulted in a marked improvement in the phasing compared with the use of super-S atoms. The VT A3 monomer consists of 46 amino acids with three disulfide bridges and has an overall fold resembling the canonical architecture of the alpha- and beta-thionins, a capital letter L. The asymmetric unit consists of two monomers related by a local twofold axis and held together by hydrophobic interactions between the monomer units. One phosphate anion (confirmed by 31P-NMR and MS) is associated with each monomer.

==About this Structure==

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[[Category: Single protein]]

[[Category: Viscum album]]

[[Category: Debreczeni, J.E.]]

[[Category: Debreczeni, J E.]]

[[Category: Girmann, B.]]

[[Category: Sheldrick, G.M.]]

[[Category: Sheldrick, G M.]]

[[Category: Zeeck, A.]]

[[Category: PO4]]

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[[Category: toxin]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of viscotoxin A3 (VT A3) extracted from European, mistletoe (Viscum album L.) has been solved using the anomalous, diffraction of the native S atoms measured in-house with Cu Kalpha, radiation to a resolution of 2.2 A and truncated to 2.5 A. A 1.75 A, resolution synchrotron data set was used for phase expansion and, refinement. An innovation in the dual-space substructure-solution program, SHELXD enabled the individual S atoms of the disulfide bonds to be located, using the Cu Kalpha data; this resulted in a marked improvement in the, phasing compared with the use of super-S atoms. The VT A3 monomer consists, of 46 amino acids with three disulfide bridges and has an overall fold, resembling the canonical architecture of the alpha- and beta-thionins, a, capital letter L. The asymmetric unit consists of two monomers related by, a local twofold axis and held together by hydrophobic interactions between, the monomer units. One phosphate anion (confirmed by 31P-NMR and MS) is, associated with each monomer.
+The crystal structure of viscotoxin A3 (VT A3) extracted from European mistletoe (Viscum album L.) has been solved using the anomalous diffraction of the native S atoms measured in-house with Cu Kalpha radiation to a resolution of 2.2 A and truncated to 2.5 A. A 1.75 A resolution synchrotron data set was used for phase expansion and refinement. An innovation in the dual-space substructure-solution program SHELXD enabled the individual S atoms of the disulfide bonds to be located using the Cu Kalpha data; this resulted in a marked improvement in the phasing compared with the use of super-S atoms. The VT A3 monomer consists of 46 amino acids with three disulfide bridges and has an overall fold resembling the canonical architecture of the alpha- and beta-thionins, a capital letter L. The asymmetric unit consists of two monomers related by a local twofold axis and held together by hydrophobic interactions between the monomer units. One phosphate anion (confirmed by 31P-NMR and MS) is associated with each monomer.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Viscum album]]
-[[Category: Debreczeni, J.E.]]
+[[Category: Debreczeni, J E.]]
 [[Category: Girmann, B.]]
-[[Category: Sheldrick, G.M.]]
+[[Category: Sheldrick, G M.]]
 [[Category: Zeeck, A.]]
 [[Category: PO4]]
@@ Line 23: / Line 23: @@
 [[Category: toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:59:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:50 2008''