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Crystallization and preliminary x-ray diffraction analysis of PD-L4, a ribosome inactivating protein from Phytolacca dioica L. leaves (131 visite)

Ruggiero A, Chambery A, Di Maro A, Pisante M, Parente A, Berisio R

Protein And Peptide Letters (ISSN: 0929-8665, 1875-5305), 2007; 14(1): 97-100.

Tipo di articolo: Journal Article, , Impact factor: 1.097, Impact factor a 5 anni: 1.019, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33846023062&partnerID=40&md5=bbc7dfc5d06a7da5757cb46c27901ddf

Parole chiave: Crystallization, Phytolacca Dioica, Ribosome Inactivating Protein, X-Ray, Pd S2 Protein, Pd-S2 Protein, Unclassified Drug, Vegetable Protein, Article, Chemistry, Isolation And Purification, Metabolism, Plant Leaf, Pokeweed, X Ray Diffraction, Plant Leaves, Plant Proteins, Type 1, X-Ray Diffraction, Phytolaccaceae,

Affiliazioni: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., I-80134 Napoli, Italy
Dipartimento di Scienze Della Vita, Seconda Università di Napoli, Via Vivaldi 43, I-81100 Caserta, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone, n. 16, I-80138 Napoli, Italy


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PD-L4, a type 1 ribosome inactivating protein from Phytolacca dioica leaves, has been successfully crystallized using vapour diffusion methods and PEG 4000 as a precipitant agent. In addition, crystals of a PD-L4 mutant, which has been recently observed to have a lower polynucleotide-adenosine glycosidase activity on DNA, rRNA and poly (A) substrates, have been obtained. To gather information on PD-L4 reaction mechanism both forms have been co-crystallized with adenine, the major product of their catalytic reaction. Diffraction patterns extend to atomic resolution and crystals belong to the orthorhombic P212121 space group, with one molecule in the asymmetric unit. Structure determination has been achieved using molecular replacement; preliminary electron density maps have clearly given evidence of adenine binding. © 2007 Bentham Science Publishers Ltd.
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Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
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Menchise V, De Simone G, Corradini R, Sforza S, Sorrentino N, Romanelli A, Saviano M, Pedone C
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Impact Factor: 2.124
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
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De Simone G, Manco G, Galdiero S, Lombardi A, Rossi M, Pavone V
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Sica F, Adinolfi S, Berisio R, De Lorenzo C, Mazzarella L, Piccoli R, Vitagliano L, Zagari A
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Impact Factor: 1.492
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Esposito L, Sica F, Sorrentino G, Berisio R, Carotenuto L, Giordano A, Raia CA, Rossi M, Lamzin VS, Wilson KS, Zagari A
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Impact Factor: 2.244
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Sica F, Adinolfi S, Vitagliano L, Zagari A, Capasso S, Mazzarella L
Cosolute effect on crystallization of two dinucleotide complexes of bovine seminal ribonuclease from concentrated salt solutions (103 visite)
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PEARL L, DEMASI D, HEMMINGS A, SICA F, MAZZARELLA L, RAIA C, DAURIA S, ROSSI M
CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF AN NAD+-DEPENDENT ALCOHOL-DEHYDROGENASE FROM THE EXTREME THERMOPHILIC ARCHAEBACTERIUM SULFOLOBUS-SOLFATARICUS (115 visite)
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39 Records (38 escludendo Abstract e Conferenze).
Impact factor totale: 63.154 (62.591 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 127.805 (127.326 escludendo Abstract e Conferenze).







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Ultimo aggiornamento: Tuesday 11 December 2018, 12:37:42