3ins

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(New page: 200px<br /><applet load="3ins" size="450" color="white" frame="true" align="right" spinBox="true" caption="3ins, resolution 1.5&Aring;" /> '''STRUCTURE OF INSULIN....)
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[[Image:3ins.gif|left|200px]]<br /><applet load="3ins" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:3ins.gif|left|200px]]<br /><applet load="3ins" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3ins, resolution 1.5&Aring;" />
caption="3ins, resolution 1.5&Aring;" />
'''STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT'''<br />
'''STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT'''<br />
==Overview==
==Overview==
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Neutron diffraction data for porcine 2Zn insulin were collected to 2.2 A, resolution from a single crystal deuterated by slow exchange of mother, liquor. A joint neutron/X-ray restrained-least-squares refinement was, undertaken using the neutron data, as well as the 1.5 A resolution X-ray, data collected previously. The final R factors were 0.182 for the X-ray, data and 0.191 for the neutron data. Resulting atomic coordinates were, compared with the initial X-ray model, showing a total r.m.s. shift of, 0.36 A for the protein and 0.6 A for the solvent. Protonation of a number, of individual amino acids was investigated by analysis of the neutron, maps. No D atoms were found between the carboxylates of Glu B13 which make, an intermolecular contact, suggesting nonbonded interaction rather than, the predicted hydrogen bond. Amide hydrogen exchange was investigated in a, refinement of their atomic occupancies. Regions of unexchanged amide, groups were found in the center of the B helices. The results of this, study emphasize the limited amount of information available in neutron, diffraction studies of proteins at resolution lower than 2 A.
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Neutron diffraction data for porcine 2Zn insulin were collected to 2.2 A resolution from a single crystal deuterated by slow exchange of mother liquor. A joint neutron/X-ray restrained-least-squares refinement was undertaken using the neutron data, as well as the 1.5 A resolution X-ray data collected previously. The final R factors were 0.182 for the X-ray data and 0.191 for the neutron data. Resulting atomic coordinates were compared with the initial X-ray model, showing a total r.m.s. shift of 0.36 A for the protein and 0.6 A for the solvent. Protonation of a number of individual amino acids was investigated by analysis of the neutron maps. No D atoms were found between the carboxylates of Glu B13 which make an intermolecular contact, suggesting nonbonded interaction rather than the predicted hydrogen bond. Amide hydrogen exchange was investigated in a refinement of their atomic occupancies. Regions of unexchanged amide groups were found in the center of the B helices. The results of this study emphasize the limited amount of information available in neutron diffraction studies of proteins at resolution lower than 2 A.
==About this Structure==
==About this Structure==
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3INS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with ZN and DOD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3INS OCA].
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3INS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=DOD:'>DOD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3INS OCA].
==Reference==
==Reference==
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[[Category: hormone]]
[[Category: hormone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:48:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:58 2008''

Revision as of 17:09, 21 February 2008

Image:3ins.gif

3ins, resolution 1.5Å

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STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT

Overview

Neutron diffraction data for porcine 2Zn insulin were collected to 2.2 A resolution from a single crystal deuterated by slow exchange of mother liquor. A joint neutron/X-ray restrained-least-squares refinement was undertaken using the neutron data, as well as the 1.5 A resolution X-ray data collected previously. The final R factors were 0.182 for the X-ray data and 0.191 for the neutron data. Resulting atomic coordinates were compared with the initial X-ray model, showing a total r.m.s. shift of 0.36 A for the protein and 0.6 A for the solvent. Protonation of a number of individual amino acids was investigated by analysis of the neutron maps. No D atoms were found between the carboxylates of Glu B13 which make an intermolecular contact, suggesting nonbonded interaction rather than the predicted hydrogen bond. Amide hydrogen exchange was investigated in a refinement of their atomic occupancies. Regions of unexchanged amide groups were found in the center of the B helices. The results of this study emphasize the limited amount of information available in neutron diffraction studies of proteins at resolution lower than 2 A.

About this Structure

3INS is a Protein complex structure of sequences from Sus scrofa with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of insulin: results of joint neutron and X-ray refinement., Wlodawer A, Savage H, Dodson G, Acta Crystallogr B. 1989 Feb 1;45 ( Pt 1):99-107. PMID:2695122

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