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10.1107/S1744309104031227 http://scihub22266oqcxt.onion/10.1107/S1744309104031227 16508111!1952408!16508111     free     free     free       Acta+Crystallogr+Sect+F+Struct+Biol+Cryst+Commun 2005 ; 61 (Pt 1): 124-7 Nephropedia Template TP {{tp|p=16508111|t=2005. Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants |pdf=|usr=}}{{16508111}} gab.com Text Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants JO: Acta Crystallogr Sect F Struct Biol Cryst Commun http://www.kidney.de/pget.php?&tw=1&pmid=16508111 #FOAvip The crystallization of three catalytically inactive mutants of penicillin V acylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide three-dimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme. Twit Text FOAVip Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants ????Acta Crystallogr Sect F Struct Biol Cryst Commun http://www.kidney.de/pget.php?&tw=1&pmid=16508111 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=16508111 #FOAvip English Wikipedia <ref>{{Cite pmid|16508111}}</ref> Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants #MMPMID16508111 Chandra PM; Brannigan JA; Prabhune A; Pundle A; Turkenburg JP; Dodson GG; Suresh CG Acta Crystallogr Sect F Struct Biol Cryst Commun 2005[Jan]; 61 (Pt 1): 124-7 PMID16508111show ga The crystallization of three catalytically inactive mutants of penicillin V acylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide three-dimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme. |Amino Acid Substitution[MESH] |Bacillus/*enzymology/genetics[MESH] |Bacterial Proteins/chemistry/genetics/isolation & purification[MESH] |Cloning, Molecular[MESH] |Crystallization[MESH] |Escherichia coli/enzymology[MESH] |Mutagenesis, Site-Directed[MESH] |Penicillin Amidase/*chemistry/genetics/isolation & purification[MESH]Cloning, preparation and preliminary crystallographic studies of penic(epmc).pdf DeepDyve Pubget Overpricing