ARC CCeMMP Research Symposium 2025

The Australian Research Council funded Centre, Centre for Cryo-electron Microscopy of Membrane Proteins (CCeMMP), is hosting a free in-person 2025 Research Symposium to showcase the exciting research and technological advances in the field of cryo-electron microscopy and membrane proteins and will feature two keynote presentations. CCeMMP invite the scientific community to attend and participate in the symposium on the 13th and 14th of November in Melbourne, Australia.

Keynote Speakers

This year, CCeMMP are excited to welcome two keynote speakers, presenting their recent cutting edge research, Professor Wai-Hong Tham and Associate Professor Alastair Stewart.

Prof. Wai-Hong Tham

Blocking Malaria Parasite Transmission: Insights from Cryo-EM of an Endogenous Fertilization Complex.
Fertilization is a critical process in generating new offspring. For malaria parasites, fertilization of its gametes occurs in the midgut of female Anopheles mosquito. By inhibiting parasite fertilization in mosquitoes, we can stop malaria parasite transmission from mosquitoes to humans. Using cryo-electron microscopy, we determined the structure of the Pfs230-Pfs48/45 core fertilization complex isolated from the sexual stages of malaria parasites.  This structure provided insight on critical domains for complex formation and led to the development of Pfs230 nanobodies and mRNA-LNP that block transmission. 

A/Prof. Alastair Stewart

Snapshots of Membrane Transport: Sodium-Dependent and Proton-Powered Proteins.

 Biological membranes serve as barriers to the external environment, allowing for selective transport and enabling energy conversion through ion gradients. This presentation explores two ion-conducting mechanisms found in membrane proteins: (i) the sodium-dependent human carnitine transporter, OCTN2 and (ii) the proton-powered bacterial ATP synthase.

(i) OCTN2 facilitates carnitine uptake across plasma membranes and is essential for fatty acid metabolism. Mutations in OCTN2 cause systemic primary carnitine deficiency (SPCD), a potentially fatal disorder. Using cryo-EM, we reveal OCTN2 maps under three conditions, identifying a sodium-binding site within an aqueous cavity distinct from the carnitine-binding pocket, as well as molecular transitions during transport. These insights, supported by electrophysiology, define the transport mechanism and provide a framework for understanding SPCD-associated variants.

(ii) ATP synthase couples proton flow to ATP production via rotary catalysis. Here we present multiple cryo-EM maps of the enzyme from Pseudomonas aeruginosa, revealing proton sub-stepping and ordered waters that support a Grotthuss mechanism for proton transfer. These molecular views also reveal separate protonation and deprotonation steps, and deepen our understanding of proton driven ATP synthesis.

Together, these findings offer molecular insights into ion transport and energy conversion, with implications for metabolic disease and antimicrobial drug development.

Program

The PDF version of the program will be available here.

Oral Presentation Abstracts

Anna Beyger, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville

Structural and pharmacological characterisation of CXCR3 isoforms and their modulation by therapeutic antagonists

Daniel Fox, Bio21, The University of Melbourne, Parkville

AI-designed protein inhibitors can block hemoglobin binding and inhibit growth of pathogenic E. coli

Dr. Rhys Grinter, Bio21, The University of Melbourne, Parkville

Quinone-transporting filaments extend the respiratory chain of Gram-positive bacteria

Dr. Joshua Hardy, The Walter and Eliza Hall Institute of Medical Research, Parkville

ProteinDJ: a high-performance and modular protein design pipeline

Kenta Ishii, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville

Integrating structural and dynamic perspectives to understand a next-gen obesity drug 

Javaid Jabbar, Bio21, The University of Melbourne, Parkville

Lysine Acetylation: A switch for OPA1-mediated membrane remodeling

Michaela Kaoullas, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville

Structural perspectives on activating the M4 muscarinic acetylcholine receptor 

Dr. Sakshi Khosa, Heinrich Heine University, Duesseldorf, Germany

Lock-and-key substrate recognition in the multidrug ABC transporter Pdr5 from Saccharomyces cerevisiae

Dr. Carus Lau, Victor Chang Cardiac Research Institute, Darlinghurst

Probing early inactivation events in hERG using the scorpion toxin CnErg1

Dr. Sarah Mueller, Australian National University, Canberra

The structural basis of nickel import in Proteus mirabilis

Dr. Fabian Munder, Bio21, The University of Melbourne, Parkville

A potent protein antibiotic kills Pseudomonas aeruginosa by inhibiting the BAM complex

Dr. Luca Troman, Bio21, The University of Melbourne, Parkville

The Pam Pilus – a novel pilus system within candidate phyla radiation bacteria

Mahmuda Yeasmin, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville

Structural basis of positive allosteric modulator selectivity at the muscarinic acetylcholine receptors

Poster Presentation Abstracts

Mechanistic insights into the activation and pore formation of insecticidal proteins from ferns

Cryo-EM structure of uPAR bound to an antibody developed for targeted cancer therapy. Implications for domain flexibility, uPA-binding and molecular Imaging

Frozen in action: Capturing vasopressin receptors in their inactive state

Understanding the assembly and structure of leukemia inhibitory factor and oncostatin-M cytokine signaling complexes

Structural basis of erythromycin binding to hERG K⁺ channels

A cryo-EM structure to unravel the unexpected promiscuity between IL-6 and IL-11Rα

Crossing the barrier: Understanding the life cycle of membrane-containing phages at molecular resolution

Towards the molecular mechanisms of ligand activation in Kv7.5 potassium ion channels

Decoding PLD3: Structural and functional discoveries with therapeutic potential for Alzheimer’s Disease

Cryo-Lamella preparation to visualise host pathogen interactions by CryoET

Visualising viral membrane fusion by SARS-CoV-2 using cryo-ET

A structural perspective on pore formation and regulation of Bacteroides fragilis toxins

A twist in the tail: The structural basis of Kv7.2/Kv7.3 channel assembly through helix D

Unravelling the structural mechanism of the pneumococcal manganese transporter PsaBCA

Mapping the unseen structural diversity of hydrogenases in silico

Structural and Functional insights on TMEM120A membrane protein

Structural insights into isoquinoline small molecule ligand-induced agonism and modulation on GLP-1R

Structural basis for non-catalytic signalling mechanisms of Eph receptor pseudokinase EphA10

Structures and dynamics of PAC1 receptor visualised in 3D animations: staying “in the loop”

Destroying the human immunodeficiency virus before infection

Structural and pharmacological validation of allosteric sites at the M₅ Muscarinic acetylcholine receptor – a target for CNS disorders

Structural analysis of new archaeal viruses

Structure and function of the GABA_B receptor upon the binding and activation by analgesic peptides

Optimized preparation of graphene-supported grids for high-resolution cryo-EM

Sponsors

This event is generously sponsored by Solve Scientific and Bio21

Organising Committee

2025 Symposium Committee Members

Dr. Ashleigh Kropp, Bio21, The University of Melbourne

Dr. Brooke Hayes, Monash University

Dr. Aidan Grosas, University of Wollongong

Dr. Naveen Vankadari Park, Bio21, The University of Melbourne

Somavally Dalvi, Bio21, The University of Melbourne

Jhonnatan Reales Gonzalez, University of Wollongong

Thomas Ficker, University of Wollongong

Supported by Dr. Tracie Pierce, Monash University

Abstract Submission Guidelines

The abstract submissions for the ARC CCeMMP Research Symposium 2025 are now closed.

Registrations for the Symposium close 5:00 PM (AEDT) October 31st, 2025.

Prizes

• CCeMMP Poster Prize – $300 AUD and a 3D printed protein model of your choice
• CCeMMP Poster Prize Runners-Up – $100 AUD
• Most Popular Oral Presentation Prize (voted by peers) – 3D printed protein model of your choice and a 2D structure print of your choice

Abstract guidelines

Please adhere to the following guidelines when submitting an abstract:

General abstract guidelines

• The submitted abstract should be relevant to the field of research i.e. membrane proteins, cryo-EM/cryo-ET work or cryo-EM/cryo-ET of membrane proteins.
• Abstracts will be maximum 300 words and maximum one A4 page in length, including any figures, photos or graphs.
• Page margins should be a minimum of 2.0 cm.
• All text should use single line spacing and full justification.
• A minimum font size of 12 point in Times New Roman.
• Abstract title should be in bold font.
• Authors should be listed and italicised.
• Address line should be included below the authors names with a space in between author names and address.
• All abstracts must be submitted and presented in English.
• Authors should indicate whether they would like to be considered for an oral presentation in the submission form (select “Poster or Oral”). The selection panel reserves the right to decide which abstracts will be presented in oral form and the length of the oral presentation.
• Upon abstract submission, you will receive an email notifying you of your successful submission.

Submit your abstract here.

Poster presentation guidelines

• Poster presentation abstract submissions have closed.
• All authors submitting abstracts will be able to present a poster.
• Posters must be presented in portrait orientation and must not exceed A0 (841 cm x 1189 cm) size. Equipment to mount posters will be provided on arrival.
• Please indicate in the Abstract Submission Form if you wish to be considered for the CCeMMP Poster Prize.

Oral presentation guidelines

• Oral presentation abstract submissions have closed.
• Please indicate in the Abstract Submission Form if you wish to be considered for an oral presentation (select “Poster or Oral”).
• Abstracts will be reviewed by a selection panel and authors selected for an oral presentation will be notified no later than Friday 17th of October 2025. The selection panel reserves the right to decide which abstracts will be presented in oral form and the length of the oral presentation.
• Oral presentations will be either 10 or 20 min in length followed by question time; you will be informed following abstract selection the length of your presentation.
• Important: Abstracts selected for an oral presentation do not need to present a poster.  If your abstract is not selected for an oral presentation, you are required to present a poster; please only submit an abstract if you are also prepared to present a poster.