From Proteopedia
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| - | [[Image:1fu2.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1fu2| PDB=1fu2 | SCENE= }} | | {{STRUCTURE_1fu2| PDB=1fu2 | SCENE= }} |
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| - | '''FIRST PROTEIN STRUCTURE DETERMINED FROM X-RAY POWDER DIFFRACTION DATA'''
| + | ===FIRST PROTEIN STRUCTURE DETERMINED FROM X-RAY POWDER DIFFRACTION DATA=== |
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| - | ==Overview==
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| - | X-ray diffraction analysis of protein structure is often limited by the availability of suitable crystals. However, the absence of single crystals need not present an insurmountable obstacle in protein crystallography any more than it does in materials science, where powder diffraction techniques have developed to the point where complex oxide, zeolite and small organic molecular structures can often be solved from powder data alone. Here, that fact is demonstrated with the structure solution and refinement of a new variant of the T(3)R(3) Zn-human insulin complex produced by mechanical grinding of a polycrystalline sample. High-resolution synchrotron X-ray powder diffraction data were used to solve this crystal structure by molecular replacement adapted for Rietveld refinement. A complete Rietveld refinement of the 1630-atom protein was achieved by combining 7981 stereochemical restraints with a 4800-step (d(min) = 3.24 A) powder diffraction pattern and yielded the residuals R(wp) = 3.73%, R(p) = 2.84%, R(F)(2) = 8.25%. It was determined that the grinding-induced phase change is accompanied by 9.5 and 17.2 degrees rotations of the two T(3)R(3) complexes that comprise the crystal structure. The material reverts over 2-3 d to recover the original T(3)R(3) crystal structure. A Rietveld refinement of this 815-atom protein by combining 3886 stereochemical restraints with a 6000-step (d(min) = 3.06 A) powder diffraction pattern yielded the residuals R(wp) = 3.46%, R(p) = 2.64%, R(F)(2) = 7.10%. The demonstrated ability to solve and refine a protein crystal structure from powder diffraction data suggests that this approach can be employed, for example, to examine structural changes in a series of protein derivatives in which the structure of one member is known from a single-crystal study.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11092920}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11092920 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11092920}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Powder diffraction]] | | [[Category: Powder diffraction]] |
| | [[Category: Rietveld refinement]] | | [[Category: Rietveld refinement]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:46:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:56:56 2008'' |
Revision as of 00:56, 1 July 2008
Template:STRUCTURE 1fu2
FIRST PROTEIN STRUCTURE DETERMINED FROM X-RAY POWDER DIFFRACTION DATA
Template:ABSTRACT PUBMED 11092920
About this Structure
1FU2 is a Protein complex structure. Full crystallographic information is available from OCA.
Reference
The first protein crystal structure determined from high-resolution X-ray powder diffraction data: a variant of T3R3 human insulin-zinc complex produced by grinding., Von Dreele RB, Stephens PW, Smith GD, Blessing RH, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1549-53. PMID:11092920
Page seeded by OCA on Tue Jul 1 03:56:56 2008
