1gh9: Difference between revisions

[[Image:1gh9.gif|left|200px]]<br /><applet load="1gh9" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1GH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry 1DW7. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH9 OCA].  

[[Category: NESG, Northeast Structural Genomics Consortium.]]

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