Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus
Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus(379 views) Ruggiero A, Squeglia F, Izzo V, Silipo A, Vitagliano L, Molinaro A, Berisio R
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Oct; 17(10): 1296-1299.
Keywords: Cell Wall, Crystal, Latency, X-Ray, Peptidoglycan, Protein Serine Threonine Kinase, Article, Chemistry, Genetics, Metabolism, Protein Binding, Staphylococcus Aureus, X Ray Crystallography, Protein-Serine-Threonine Kinases, Bacteria (microorganisms),
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, CNR, Napoli, Italy
University of Naples Federico II, Napoli, Italy
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Matthews, B. W., Solvent content of protein crystals (1968) J. Mol. Biol, 33, pp. 491-497
McCoy, A. J., Solving structures of protein complexes by molecular replacement with phaser (2007) Acta. Crystallogr. D. Biol. Crystallogr, 63, pp. 32-41
Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus
Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus
Expression, purification, crystallization and preliminary x-ray crystallographic analysis of the peptidoglycan binding region of the ser/thr kinase PrkC from staphylococcus aureus
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