A collection of more than 1800 carbonized papyri, discovered in the Roman ‘Villa dei Papiri’ at Herculaneum is the unique classical library survived from antiquity. These papyri were charred during 79 A.D. Vesuvius eruption, a circumstance which providentially preserved them until now. This magnificent collection contains an impressive amount of treatises by Greek philosophers and, especially, Philodemus of Gadara, an Epicurean thinker of 1st century BC. We read many portions of text hidden inside carbonized Herculaneum papyri using enhanced X-ray phase-contrast tomography non-destructive technique and a new set of numerical algorithms for ‘virtual-unrolling’. Our success lies in revealing the largest portion of Greek text ever detected so far inside unopened scrolls, with unprecedented spatial resolution and contrast, all without damaging these precious historical manuscripts. Parts of text have been decoded and the ‘voice’ of the Epicurean philosopher Philodemus is brought back again after 2000 years from Herculaneum papyri.

We demonstrate for the first time the viability of a three-dimensional (3D) elemental imaging technique based on Neutron Resonance Transmission Imaging (NRTI), which is a neutron technique based on the presence of a resonance structure in the neutron-induced reaction cross sections. These resonances allow the identification of elements and isotopes within an object in a non-destructive manner. A dedicated set-up on the INES (Italian Neutron Experimental Station) beamline of the ISIS spallation neutron source was employed for the experiments. An early mediaeval disc fibula from the Hungarian National Museum in Budapest was used for our demonstration. The methodology and analysis procedures are described and the results obtained from the reconstruction of the 3D NRTI elemental image of the ancient object are compared with the results obtained from other neutron-based 3D imaging techniques.

Neutron resonances are the signature signals of a non-destructive elemental and isotopic analysis technique in archaeological sciences. We report on Neutron Resonance Transmission Analysis and its capabilities as a bulk elemental imaging technique to test the homogeneity of samples and to localize elements of interest in archaeological samples and museum objects. A high neutron flux is required for imaging in order to achieve reasonable spatial resolution and to keep measurement times within realistic limits. A modular system for neutron resonance transmission analysis has been designed and installed at the INES beamline of the ISIS spallation neutron source as a part of the ANCIENT CHARM project. The main component is a neutron position sensitive transmission detector which is based on a 10 × 10 array of ⁶Li-glass crystals mounted on a pitch of 2.5 mm, resulting in a 25 × 25 mm² active area. Transmission spectra are obtained by a measurement of the flight time of epithermal neutrons passing through an object. The transmission dips observed in a time-of-flight spectrum can be used to identify and quantify specific nuclides. In this paper the technique is described together with the data reduction and analysis procedures. In addition, preliminary results obtained from measurements on cultural heritage samples are discussed.

Aggregation states of amyloid beta peptides for amyloid beta A $\beta$ ${}_{1–40}$ to A $\beta$ ${}_{1–42}$ and A $\beta$ p ${}_{3–42}$ are investigated through small angle neutron scattering (SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer’s disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomers and fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radius of gyration of the order of 10 Å, while the oligomers and fibrils display differences in size and aggregation ability, with A $\beta$ p ${}_{3–42}$ showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloid peptide and indeed to the development of the associated disease.