Search Results

You searched for all publications:

with publication states 'Published' 'Published (Approved)'

Search Again...

These results include publications that have not yet been reviewed and processed by Diamond Light Source. To view only processed publications click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

2 items found (0 items not approved), displaying all items.1

Instruments / Technical Area	Publication Details	Published	Actions
I12-JEEP: Joint Engineering, Environmental and Processing	Synchrotron characterisation of ultra-fine grain TiB2/Al-Cu composite fabricated by laser powder bed fusion Sheng Li , Biao Cai , Ranxi Duan , Lei Tang , Zihan Song , Dominic White , Oxana Magdysyuk , Moataz M. Attallah Acta Metallurgica Sinica (english Letters) 23 DOI: 10.1007/s40195-021-01317-y Diamond Proposal Number(s): [22506] Open Access Show Abstract ▼ Abstract: Isotropy in microstructure and mechanical properties remains a challenge for laser powder bed fusion (LPBF) processed materials due to the epitaxial growth and rapid cooling in LPBF. In this study, a high-strength TiB2/Al-Cu composite with random texture was successfully fabricated by laser powder bed fusion (LPBF) using pre-doped TiB2/Al-Cu composite powder. A series of advanced characterisation techniques, including synchrotron X-ray tomography, correlative focussed ion beam–scanning electron microscopy (FIB-SEM), scanning transmission electron microscopy (STEM), and synchrotron in situ X-ray diffraction, were applied to investigate the defects and microstructure of the as-fabricated TiB2/Al-Cu composite across multiple length scales. The study showed ultra-fine grains with an average grain size of about 0.86 μm, and a random texture was formed in the as-fabricated condition due to rapid solidification and the TiB2 particles promoting heterogeneous nucleation. The yield strength and total elongation of the as-fabricated composite were 317 MPa and 10%, respectively. The contributions of fine grains, solid solutions, dislocations, particles, and Guinier–Preston (GP) zones were calculated. Failure was found to be initiated from the largest lack-of-fusion pore, as revealed by in situ synchrotron tomography during tensile loading. In situ synchrotron diffraction was used to characterise the lattice strain evolution during tensile loading, providing important data for the development of crystal-plasticity models.	Sep 2021
I03-Macromolecular Crystallography	The X-ray structure of juvenile hormone diol kinase from the silkworm Bombyx mori Jingxu Guo , Ronan M. Keegan , Daniel J. Rigden , Peter T. Erskine , Steve P. Wood , Sheng Li , Jonathan B. Cooper Acta Crystallographica Section F Structural Biology Communications 77 DOI: 10.1107/S2053230X21012012 Diamond Proposal Number(s): [12342] Show Abstract ▼ Abstract: Insect juvenile hormones (JHs) are a family of sesquiterpenoid molecules that are secreted into the haemolymph. JHs have multiple roles in insect development, metamorphosis and sexual maturation. A number of pesticides work by chemically mimicking JHs, thus preventing insects from developing and reproducing normally. The haemolymph levels of JH are governed by the rates of its biosynthesis and degradation. One enzyme involved in JH catabolism is JH diol kinase (JHDK), which uses ATP (or GTP) to phosphorylate JH diol to JH diol phosphate, which can be excreted. The X-ray structure of JHDK from the silkworm Bombyx mori has been determined at a resolution of 2.0 Å with an R factor of 19.0% and an Rfree of 24.8%. The structure possesses three EF-hand motifs which are occupied by calcium ions. This is in contrast to the recently reported structure of the JHDK-like-2 protein from B. mori (PDB entry 6kth), which possessed only one calcium ion. Since JHDK is known to be inhibited by calcium ions, it is likely that our structure represents the calcium-inhibited form of the enzyme. The electrostatic surface of the protein suggests a binding site for the triphosphate of ATP close to the N-terminal end of the molecule in a cavity between the N- and C-terminal domains. Superposition with a number of calcium-activated photoproteins suggests that there may be parallels between the binding of JH diol to JHDK and the binding of luciferin to aequorin.	Dec 2021

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User