1g50: Difference between revisions

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-[[Image:1g50.gif|left|200px]]
+{{Seed}}
+[[Image:1g50.png|left|200px]]
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 {{STRUCTURE_1g50|  PDB=1g50  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION'''
+===CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION===
-==Overview==
+<!--
-Several crystal structures of human estrogen receptor alpha ligand-binding domain (hERalpha LBD) complexed with agonist or antagonist molecules have previously been solved. The proteins had been modified in cysteine residues (carboxymethylation) or renatured in urea to circumvent aggregation and denaturation problems. In this work, high-level protein expression and purification together with crystallization screening procedure yielded high amounts of soluble protein without renaturation or modifications steps. The native protein crystallizes in the space group P3(2) 21 with three molecules in the asymmetric unit. The overall structure is very similar to that previously reported for the hERalpha LBD with cysteine carboxymethylated residues thus validating the modification approach. The present strategy can be adapted to other cases where the solubility and the proper folding is a difficulty.
+The line below this paragraph, {{ABSTRACT_PUBMED_11437591}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11437591 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11437591}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Structural proteomics in europe]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:06:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:26:02 2008''