Scientific Seminars

Below is a list of upcoming seminars at the LMB aimed at a general scientific audience and open to individuals throughout Cambridge. If you are not at the LMB and wish to attend a seminar, please contact Nikki Dominguez.

The LMB hosts ‘The LMB Seminar Series’, where 1-2 leading scientists per month are invited to speak throughout the year. Four of these lectures are named in honour of LMB Nobel Laureates Max Perutz, Francis Crick, César Milstein and John Kendrew, given by eminent scientists from around the world. The LMB Seminar talks and LMB Named Seminar talks are advertised widely throughout the local area and are open to all.

2017 LMB Seminar Series speakers (click to expand)

  • Margaret Goodell – 11:15am, 20th June 2017
  • Andreas Matouschek – 4pm, 3rd July
  • Chris Lima – 11am, 14th July
  • Patrick Cramer – 4pm, 5th September
  • Jack Szostak – 4pm, 7th September (Crick Lecture)
  • Susan Lea – 11am, 2nd October
  • Erin O’Shea – 11am, 15th November (Perutz Lecture)
  • Michelle Dunstone – 12th December

 

A full list of LMB Named Lectures to date can be found here.

Details of other local seminars can be found here


  • LMB cryo-EM course - Tomography

    Speaker: John Briggs, MRC LMB
    Host: Sjors Scheres, MRC LMB
    Date: 29/06/2017 at 9:30am in the Max Perutz Lecture Theatre, LMB.


  • A synthetic base-triple motif for nucleic acid structure-function control and delivery

    Speaker: Professor Dennis Bong, Department of Chemistry & Biochemistry, The Ohio State University, USA
    Host: Madan Babu Mohan, MRC LMB
    Date: 29/06/2017 at 11:30am in the Sanger Seminar Room, Level 3, LMB.

    Further information

    We have recently reported the use of triaminotriazine (melamine) as a synthetic base-triple motif in a family of molecules we call bifacial peptide nucleic acid (bPNA). Bifacial PNA engages two oligo T/U strands simultaneously to form a unique triple stranded structure. We demonstrate functional compatibility of bPNA with functional non-coding DNA and RNA scaffolds by the use of bPNA as an allosteric trigger of aptamer protein-binding, ribozyme catalysis, aptamer small-molecule binding and potent siRNA delivery. Peptoid, polyacrylate and small molecules have all been demonstrated to be functional nucleic acid hybridization scaffolds. Small molecules displaying melamine can target T/U bulges in folded nucleic acid structures and trigger cooperative folding in unstructured oligo T/U domains. We have found that G-quadruplex based RNA aptamers may be engineered to yield alter fluorogen-binding selectivity using melamine targeting; similarly, the hammerhead ribozyme has been engineered to respond to melamine-based small molecule synthetic allosteric switches. Overall, this work describes the wide range of applications emerging from the use of a simple artificial base triple unit.

  • LMB cryo-EM course - Local setup and training

    Speaker: Shaoxia Chen/Giuseppe Cannone, MRC LMB
    Host: Sjors Scheres, MRC LMB
    Date: 30/06/2017 at 9:30am in the Max Perutz Lecture Theatre, LMB.


  • Annual AWiSE-LMB Lunchtime Careers Meeting

    Speaker: Monika Papworth, Antibody Discovery and Protien Engineering at MadImmune: Sarah Cumbers, Associate Director Guidance Transformation at NICE and Elizabeth Fairley, Director of Talking Medicines
    Host: Cambridge AWiSE-LMB
    Date: 30/06/2017 at 12:00pm in the Max Perutz Lecture Theatre, LMB.

    Further information

    To register please go to https://www.eventbrite.co.uk/e/what-next-for-your-career-the-annual-lmb-camawise-careers-event-2017-registration-35458348876

    Are you wondering how to best utilise your scientific skills? Are you planning your next step in academia or considering pursuing a career away from the bench? Would you like more information about different scientific careers from a diverse range of speakers?

    The LMB’s annual careers event will take place on Friday 30th June, 12-2pm, in the Max Perutz Lecture Theatre.

    The speakers will give their talks with the opportunity for questions, followed by a buffet lunch, which will provide time for networking and gaining advice about making that next step.

    This meeting is held in collaboration with Cambridge AWiSE. All are welcome and the event is free to attend, but please register.

  • Towards structural characterization of cell surface signalling assemblies

    Speaker: Doctor Dimple Karia, Division of Structural Biology, University of Oxford
    Host: Lori Passmore, MRC LMB
    Date: 03/07/2017 at 10:30am in the Klug Seminar Room, Level 2, LMB.

    Further information

    Cell migration plays a crucial role in various biological processes such as embryonic development, immune responses and tissue regeneration in all multicellular organisms. It also plays an important role in pathological processes like cancer metastasis. The process of cell migration relies upon extracellular guidance cues. These secreted or membrane attached molecules interact with the cell surface receptors to direct attractive or repulsive cellular responses. There are four major classes of cell guidance cues; ephrins, semaphorins, slits and netrins. I am primarily working on Eph-ephrin and Plexin-semaphorin signalling assemblies.

    Eph receptors constitute the largest subfamily of receptor tyrosine kinases and along with their ephrin ligands play a crucial role in mediating cell-cell communication, regulating cell attachment, shape and mobility. The aim is to understand the structure of EphA2 full length receptor in isolation and in complex with its ligand, ephrinA5. EphA2 is 110kDa single pass transmembrane protein. Detergent screening and thermostability assays allowed selection of the most suitable conditions for extraction of the protein from cell membranes. Negative stain TEM and 2D classification showed the protein to be filamentous. I am using various approaches such as membrane protein enriched extracellular vesicles (MPEEVs) and saposin- lipoprotein nanoparticle system (Salipro) for sample preparation for CryoEM single particle analysis and Cryoelectron tomography. Initial results indicated successful incorporation of the EphA2 protein into Salipro.

    Similarly, semaphorins are a large family of membrane bound and secreted proteins playing a vital role as cell guidance cues in a wide range of physiological and pathological processes such as vasculogenesis, angiogenesis, immune response, cardiogenesis and tumour metastasis. Semaphorins signal in conjunction with their receptors, plexins and coreceptors, neuropilins. In parallel I am also working on structure characterisation of PlexinD1- Semaphorin3E complex (expected to form a 500kDa 2:2 complex) using CryoEM single particle analysis. Initial 2D classes from single particle analysis show the tetrameric complex formation. However, there is a problem of aggregation and preferential orientation. I am in process of further optimizing the sample to address these issues.

    Structural characterization of these receptor-ligand signalling complexes will give us mechanistic insights into their functions which will provide stepping stones for targeting these receptors for therapeutics.

  • Time-resolved diffraction experiments at X-ray free electron lasers reveal structural changes in bacteriorhodopsin and a bacterial photosynthetic reaction centre

    Speaker: Professor Richard Neutze, University of Gothenburg, Sweden
    Host: Richard Henderson, MRC LMB
    Date: 03/07/2017 at 2:30pm in the Klug Seminar Room, Level 2, LMB.

    Further information

    X-ray free electron lasers (XFEL) provide a billion-fold jump in the peak X-ray brilliance compared with synchrotron radiation. One area where XFEL radiation is having an impact is time-resolved structural studies of protein conformational changes. In this presentation I will discuss the key ideas underlying the application of XFEL radiation to structural studies of biomolecules. I will then describe in detail two projects where we have used time resolved serial femtosecond crystallography at an XFEL to probe light driven structural changes in energy transducing membrane proteins:bacteriorhodopsin and a bacterial photosynthetic reaction centre.

    Bacteriorhodopsin is a light-driven proton pump which has long been used as a model system in biophysics. The mechanism by which light-driven isomerization of a retinal chromophore is coupled to the transport of protons “up-hill” against a transmembrane proton concentration gradient involves protein structural changes. Collaborative studies at SACLA have probed structural changes in microcrystals on a time-scale from nanoseconds to milliseconds. Structural results from these studies enabled a complete picture of structural changes occurring during proton pumping by bacteriorhodopsin to be recovered (Nango et al., 2016).

    The photosynthetic reaction centre of Bl. viridis is also an integral membrane protein that harvests sunlight to pump protons. Proton transport is achieved through the movement of electrons across the cell membrane and these electron movements are coupled to redox reactions. Time resolved diffraction studies at LCLS revealed structural changes on the picosecond time-scale near the special pair and the tightly bound menaquinone. These structural results provide chemical insight into two biophysical mechanisms by which the energy of sunlight is directed into the biosphere.

  • LMB Seminar Series - How the proteasome selects proteins for degradation

    Speaker: Andreas Matouscheck, Northwestern University, USA
    Host: Madan Babu
    Date: 03/07/2017 at 4:00pm in the Max Perutz Lecture Theatre, LMB.

    Further information

    The ubiquitin proteasome system adjusts cellular protein concentrations by selecting proteins and hydrolyzing them into peptides. At the center of this system is the proteasome, a protein machine that can degrade effectively any protein but does so with exquisite specificity. Proteins are targeted to the proteasome through through ubiquitin tags but degradation begins at disordered regions elsewhere in the proteins. The proteasome thus has to recognize two sites in its substrates and both steps contribute to the specificity of degradation. We are determining how the proteasome recognizes the two parts of the degradation signal and how the recognition rules we define biochemically govern physiological protein degradation in cells. Finally, we apply the mechanistic insights we gain to design tools to deplete proteins from cells artificially.

  • Study the roles of Atg8s in autophagy

    Speaker: Professor Zvulun Elazar, Weizmann Institute
    Host: Felix Randow
    Date: 05/07/2017 at 12:00am in the Sanger Seminar Room, Level 3, LMB.


  • Structure and dynamics of the neurotensin receptor NTSR1

    Speaker: Doctor Reinhard Grisshammer, National Institute of Neurological Disorders and Stroke, NIH, Rockville, USA
    Host: Chris Tate
    Date: 12/07/2017 at 2:00pm in the Max Perutz Lecture Theatre, LMB.

    Further information

    Previously, we have determined the crystal structure of a thermostabilized NTSR1 mutant (NTSR1-GW5) in an active-like conformation, bound to the ligand neurotensin, providing for the first time insight into the binding mode of a peptide agonist to a GPCR. To further gain insight into the NTSR1 activation mechanism, we performed extensive pharmacological studies and subsequently determined the crystal structures of two additional mutants: NTSR1-LF, which is partially active at the Gq protein in response to agonist, and NTSR1-ELF, which is active. In addition, we have determined the structure of a constitutively active NTSR1 mutant, which signals in the absence of an agonist. Together, our structures provide a framework to understand the structural features essential for activating G protein by NTSR1 as a representative of a peptide GPCR.

  • G protein-coupled receptors: structure-based drug discovery from crystals to the clinic

    Speaker: See Further Information for a list of speakers
    Host: Chris Tate
    Date: 13/07/2017 at 10:00am in the Max Perutz Lecture Theatre, LMB.

    Further information

    In celebration of the 10th Anniversary of the founding of Heptares Therapeutics.

    10.00 am - 5.30 pm

    Speakers:
    Fiona Marshall, Heptares Therapeutics
    Malcolm Weir, Heptares Therapeutics
    Chris Tate, MRC LMB
    Richard Henderson, MRC LMB
    Gebhard Schertler, Paul-Scherrer Institute, Villigen
    Andreas Plückthun, ETH, Zurich
    Rob Cooke, Heptares Therapeutics
    Jon Mason, Heptares Therapeutics
    Tim Tasker, Heptares Therapeutics
    Miles Congreve, Heptares Therapeutics

    Everyone is welcome to come to the meeting, which is free and will be held
    in the Max Perutz Lecture Theatre. However, space is limited, so it is
    essential to book online at http://bit.ly/2iDetPV within the next few
    weeks so that we can make appropriate arrangements.

    Email Chris Tate on cgt@mrc-lmb.cam.ac.uk

  • LMB Seminar Series- Title to follow

    Speaker: Chris Lima
    Host: David Komander
    Date: 14/07/2017 at 11:00am in the Max Perutz Lecture Theatre, LMB.


  • Single-molecule dissection of cytoplasmic dynein tension sensing and force generation.

    Speaker: Doctor Arne Gennerich, Dept of Anatomy and Structural Biology, Albert Einstein College of Medicine, Edinburgh
    Host: Andrew Carter, MRC LMB
    Date: 19/07/2017 at 11:00am in the Klug Seminar Room, Level 2, LMB.

    Further information

    Cytoskeletal motor protein motility requires coordination of ATPase and filament-binding cycles. Mechanical tension, which arises from both external and intramolecular forces, regulates motor stepping. In cytoplasmic dynein –a unique AAA+ ATPase with six linked AAA+ domains, a coiled coil stalk that connects the AAA+ ring and microtubule (MT)-binding domains, and a dimerizing tail domain– applied tension affects MT-binding strength anisotropically, with backward tension inducing stronger binding. In this seminar, I will present our most recent combined structure-function and optical tweezers studies that provide new insights into how dynein senses directional tension and into how dynein’s motors domains coordinate their movements. In addition, I will discuss the evolutionary differences in the force generation of metazoan and non-metazoan dyneins.

  • LMB Seminar Series-Title to follow

    Speaker: Patrick Cramer, Max Planck Institute
    Host: Phil Holliger
    Date: 05/09/2017 at 11:00am in the Max Perutz Lecture Theatre, LMB.


  • Crick Lecture-title to follow

    Speaker: Jack Szostak, Harvard, USA
    Host: Phil Holliger
    Date: 07/09/2017 at 4:00pm in the Max Perutz Lecture Theatre, LMB.


  • LMB Seminar-Title to follow

    Speaker: Susan Lea,
    Host: Andrew Carter
    Date: 02/10/2017 at 11:00am in the Max Perutz Lecture Theatre, LMB.


  • Max Perutz Lecture

    Speaker: Erin O Shea, Howard Hughes Medical Institute
    Host: Liz Miller
    Date: 15/11/2017 at 11:00am in the Max Perutz Lecture Theatre, LMB.