ACTIVE SITE TARGETING OF PROTEIN TYROSINE PHOSPHATASES BY SYNCH CRYSTALLOGRAPHY
$0P41FY2002RRNIH
Yeshiva University, New York NY
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Abstract
RNA 3'-terminal phosphate cyclase catalyzes the ATP-dependent conversion of the 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. It is an essential enzyme and conserved across all kingdoms. Data were collected for a crystal of RNA 3' Phosphate cyclase soaked in the solution containing 10mM AMP. Data collection statistics: 97% completeness at 3 A resolution and the R-factor (20 A - 3A) is 5.7. Unfortunately, it does not appear that AMP was bound with detectable occupancy.
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