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Acta crystallographica Section F Structural biology communications



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Titolo: Acta crystallographica Section F Structural biology communications Visualizza cluster
Pubblicazione: Malden, MA : , : John Wiley & Sons Inc., , [2014]-
Descrizione fisica: 1 online resource
Disciplina: 548
Soggetto topico: Macromolecular Substances
Crystallography
Crystallization
Soggetto genere / forma: Fulltext
Internet Resources.
Periodicals.
Periodical
Note generali: Refereed/Peer-reviewed
Nota di contenuto: Crystals on the cover 2014 -- Introduction to protein crystallization -- Structural mechanism of DNA recognition by the p202 HINa domain: insights into the inhibition of Aim2-mediated inflammatory signalling -- The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 Å resolution -- Structures of adenosine kinase from Trypanosoma brucei brucei -- Structure of Mycobacterium tuberculosis nucleoside diphosphate kinase R80N mutant in complex with citrate -- Crystallization and preliminary X-ray analysis of a complex of the FOXO1 and Ets1 DNA-binding domains and DNA -- Purification, crystallization and preliminary X-ray diffraction analysis of a novel keto-deoxy-d-galactarate (KDG) dehydratase from Agrobacterium tumefaciens -- Expression, purification, crystallization and preliminary X-ray diffraction studies of phosphoglycerate mutase from Staphylococcus aureus NCTC8325 -- Cloning, purification, crystallization and preliminary X-ray studies of HMO2 from Saccharomyces cerevisiae -- Crystallization and preliminary X-ray study of Vibrio cholerae uridine phosphorylase in complex with 6-methyluracil -- Purification, crystallization and preliminary X-ray analysis of an HA17-HA70 (HA2-HA3) complex from Clostridium botulinum type C progenitor toxin -- Purification, crystallization and preliminary X-ray diffraction of the N-terminal calmodulin-like domain of the human mitochondrial ATP-Mg/Pi carrier SCaMC1 -- Crystallization and preliminary X-ray diffraction studies of a surface mutant of the middle domain of PB2 from human influenza A (H1N1) virus -- Crystallization and preliminary X-ray crystallographic analysis of the small subunit of the heterodimeric laccase POXA3b from Pleurotus ostreatus -- Cloning, expression, purification and preliminary X-­ray crystallographic analysis of mouse protein arginine methyltransferase 7 -- Expression, purification, crystallization and preliminary X-ray diffraction analysis of the novel modular DNA-binding protein BurrH in its apo form and in complex with its target DNA -- Expression, crystallization and preliminary X-ray diffraction analysis of thioredoxin glutathione reductase from Schistosoma japonicum in complex with FAD -- Cloning, overexpression, purification and preliminary X-ray analysis of a feast/famine regulatory protein (Rv2779c) from Mycobacterium tuberculosis H37Rv -- Crystallization and preliminary X-ray diffraction analysis of FabG from Yersinia pestis -- Preliminary X-ray diffraction analysis of thermostable β-1,4-xylanase from Streptomyces sp. S9 -- Crystallization and preliminary X-ray crystallographic analysis of l-arabinose isomerase from thermophilic Geobacillus kaustophilus -- Purification, crystallization and preliminary X-ray crystallographic analysis of a rice Rac/Rop GTPase, OsRac1 -- Crystallization and structure determination of a symmetrical 'football' complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins -- Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of recombinant human fumarase -- Purification, crystallization and preliminary X-ray analysis of the inverse F-BAR domain of the human srGAP2 protein -- Measurement of the intrinsic variability within protein crystals: implications for sample-evaluation and data-collection strategies.
Titolo abbreviato (Periodici): ACTA CRYSTALLOGR F STRUCT BIOL COMMUN
Acta Crystallogr F Struct Biol Commun
Altri titoli varianti: Structural biology communications
Acta crystallographica F
Titolo autorizzato: Acta crystallographica  Visualizza cluster
Formato: Materiale a stampa
Livello bibliografico Periodico
Lingua di pubblicazione: Inglese
Record Nr.: 9910132521103321
Lo trovi qui: Univ. Federico II
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