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| {{STRUCTURE_1eje| PDB=1eje | SCENE= }} | | {{STRUCTURE_1eje| PDB=1eje | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF AN FMN-BINDING PROTEIN'''
| | ===CRYSTAL STRUCTURE OF AN FMN-BINDING PROTEIN=== |
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| ==Overview==
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| A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11017201}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11017201 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11017201}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Psi]] | | [[Category: Psi]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:10:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:50:27 2008'' |