[ccp4bb] Postdoctoral Research Fellow vacancy - protein kinases in Bayliss lab, Leeds
I am looking for a Postdoctoral Research Fellow to explore the regulation of protein kinases and to contribute structural insights to drug discovery projects. The catalytic activities of protein kinases are controlled through protein-protein interactions and post-translational modifications. The project aims to resolve the structural basis of these mechanisms using a combination of protein crystallography, biochemistry, computational biology and biophysical approaches. The insights gleaned from these studies will underpin the development of allosteric kinase inhibitors. The post is funded by a Programme Award from Cancer Research UK, and is available until 28 February 2020 in the first instance, renewable for a further 2 years Informal enquiries welcome - follow the link to apply https://jobs.leeds.ac.uk/vacancy.aspx?ref=FBSMB1132 === Prof. Richard Bayliss Head of the School of Molecular and Cellular Biology Professor of Molecular Medicine Faculty of Biological Sciences Astbury Building University of Leeds Leeds LS2 9JT Email: r.w.bayl...@leeds.ac.uk Tel: 0113 3439919 Twitter: @baylisslab [cid:4AACB59B-0660-4C7C-B997-79F621AF1292]
[ccp4bb] Postdoctoral Research Fellow vacancy in Leeds
Research Fellow in Structural and Computational Biology Many of the proteins that are critical for cancer development are intrinsically disordered or have large disordered regions. Moreover, the genetic alterations that promote cancer generate mutated forms of proteins that are destabilized. One example is the fusion protein formed from the microtubule binding protein EML4 and the tyrosine kinase ALK. The EML4-ALK fusion is the key driver in approximately 5% of non-small cell lung cancer (NSCLC) patients. Alternative breakpoints in the EML4 gene result in fusion proteins of different lengths and properties, and patients with longer forms respond better to treatment that those with shorter forms. We do not understand why this is the case, but we hypothesize that it is due to differences in protein stability and protein-protein interactions. The longer forms of EML4-ALK, found in two-thirds of patients, include only part of a tandem beta propeller (TAPE) domain. The broken TAPE domain does not impede the expression of the fusion protein, or inhibit the catalytic activity of the fused ALK kinase, and contributes directly to cancer signaling. This is remarkable because the folding of the broken TAPE domain should be severely compromised. We are looking for a Research Fellow to explore the structural dynamics and interactions of disordered regions of proteins of relevance to cancer, starting with the broken TAPE domain of EML4-ALK. You will explore the structure and dynamics of the broken TAPE domain in the fusion protein, characterize its molecular interactions and decipher the molecular mechanisms that underpin cancer signaling. Approaches will include molecular simulation, biophysical characterization of protein folding and advanced mass spectrometry. We have a long-standing interest in intrinsically disordered proteins and their interactions, protein kinases and cancer signalling. The post is funded by a Programme Award from Cancer Research UK, which supports a thriving research group embedded in the Astbury Centre<http://www.astbury.leeds.ac.uk/> for Structural and Molecular Biology. To explore the post further or for any queries you may have, please contact: Richard Bayliss<http://www.astbury.leeds.ac.uk/people/staff/staffpage.php?StaffID=RWB>, Professor of Molecular Medicine Tel: +44 (0)113 343 9919, email: <mailto:r.w.bayl...@leeds.ac.uk> r.w.bayl...@leeds.ac.uk<mailto:r.w.bayl...@leeds.ac.uk> Location: Leeds - Main Campus Faculty/Service:Faculty of Biological Sciences School/Institute: School of Molecular & Cellular Biology Category: Research Grade: Grade 7 Salary: £32,548 to £38,833 p.a. Due to funding limitations an appointment cannot be made above £34,520 p.a. Working Time: 100% Post Type: Full Time Contract Type: Fixed Term (until 28 February 2020, potential to extend for further 24 months - due to funding) Closing Date: Tuesday 02 January 2018
[ccp4bb] PhD studentship in structural/cell biology at the University of Leicester
A 3-year PhD studentship is available from October 2011 in the Biochemistry Department at the University of Leicester on Structural and functional studies on mitotic NIMA-related kinases. The student will be based jointly in the laboratories of Richard Bayliss (bayliss...@me.com) and Andrew Fry (a...@le.ac.uk), and informal enquiries can be sent to either supervisor. NIMA-related kinases are key regulators of mitosis, centrosomes and microtubules, and are a major focus of both laboratories. The Bayliss and Fry laboratories are housed within the flagship Henry Wellcome Building on the main University campus and are served by state-of-the-art facilities in structural biology and fluorescence microscopy. This project will provide the student with an excellent grounding in cutting-edge biochemical and molecular cell biology techniques. Hard-working, independent- minded and enthusiastic students who can work well in a team are encouraged to apply. For examples of our recent work relevant to the project see: 1) Richards MW, O’Regan L, Mas-Droux C, Blot JMY, Cheung J, Hoelder S, Fry AM, Bayliss R. (2009) An auto-inhibitory tyrosine motif in the cell cycle-regulated Nek7 kinase is released through binding of Nek9. Mol. Cell. 36(4):560-70. 2) O'Regan L, Fry AM. (2009). The Nek6 and Nek7 protein kinases are required for robust mitotic spindle formation and cytokinesis. Mol Cell Biol. 29(14):3975-90. Project details: http://www2.le.ac.uk/colleges/medbiopsych/research/studentships/research-studentships-2011/MBSP-11-02%20Bayliss.pdf Bayliss lab website: http://web.mac.com/baylisslab Fry lab website: http://www2.le.ac.uk/departments/biochemistry/staff/fry Departmental website: http://www2.le.ac.uk/departments/biochemistry/research Eligibility: these awards are open to all applicants, but International applicants (i.e. non UK/EU nationals/permanent residents) will be required to pay the difference between the International Registration fee (approx £9,500 p/a) The Institute of Cancer Research: Royal Cancer Hospital, a charitable Company Limited by Guarantee, Registered in England under Company No. 534147 with its Registered Office at 123 Old Brompton Road, London SW7 3RP. This e-mail message is confidential and for use by the addressee only. If the message is received by anyone other than the addressee, please return the message to the sender by replying to it and then delete the message from your computer and network.
Re: [ccp4bb] Cryoprotection in 3M ammonium sulfate
I third it - we used 3.2M + 5% glycerol ammonium sulfate to cryoprotect crystals grown in 1.2M ammonium suphate (Bayliss et al. JBC 2002). This really helped diffraction too. My tip when handling drops at very high salt is to make a little circle of wet tissue paper around your coverslip to make a humidity chamber. You'll have much longer to fish crystals out of the drop before salt crystals start to form. Good luck Richard Dr Richard Bayliss Royal Society University Research Fellow Career Development Team Leader Section of Structural Biology Institute of Cancer Research 237 Fulham Road London SW3 6JB UK Tel: +44 (0)20 71535557 Fax: +44 (0)20 71535457 On 19 Aug 2009, at 7:20 PM, James Holton wrote: I second that one. Ammonium sulfate is one of my favorite cryos. I recommend making up a saturated solution of ammonium sulfate, as it is actually a very good cryo all by itself, and then dilute it by adding the rest of the stuff in your condition (buffers, etc. and a little bit of water). You want to be a little below saturation so that the salt does not grow crystals of its own while you are soaking. This is especially important if your protein crystals are hexagonal rods! -James Holton MAD Scientist Savvas Savvides wrote: Hi Brenda Try 3M ammonium sulfate itself! We have tried that with great succes by cryo-cooling xtals grown at 3.2M AS straight out of their crystallization drops. You can consult the MM section in Kyndt J. et al Biochemistry 2007 Jan 9;46(1):95-105 for a more detailed description of what we did. Best of luck Savvas Savvas Savvides L-ProBE, Unit for Structural Biology Ghent University K.L. Ledeganckstraat 35 9000 Ghent, BELGIUM office: +32- (0)9-264.51.24 ; mobile: +32-(0)472-92.85.19 Email: savvas.savvi...@ugent.be http://www.lprobe.ugent.be/xray.html -Original Message- From: CCP4 bulletin board [mailto:ccp...@jiscmail.ac.uk] On Behalf Of Schulman, Brenda Sent: Wednesday, August 19, 2009 6:19 PM To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] Cryoprotection in 3M ammonium sulfate Hello! I would be grateful for suggestions on cryoprotectants for crystals growing in 3M ammonium sulfate. Thanks! Brenda Email Disclaimer: www.stjude.org/emaildisclaimer E-mail message checked by Spyware Doctor (6.1.0.447) Database version: 6.13080 http://www.pctools.com/en/spyware-doctor-antivirus/ The Institute of Cancer Research: Royal Cancer Hospital, a charitable Company Limited by Guarantee, Registered in England under Company No. 534147 with its Registered Office at 123 Old Brompton Road, London SW7 3RP. This e-mail message is confidential and for use by the addressee only. If the message is received by anyone other than the addressee, please return the message to the sender by replying to it and then delete the message from your computer and network.
[ccp4bb] Postdoc position at the Institute of Cancer Research, London
Post Doctoral Training Fellow Section of Structural Biology, The Institute of Cancer Research The Institute of Cancer Research (a College of the University of London) is a world-class cancer research organization with HEFCE RAE ratings of international excellence across all of its research programmes. In partnership with The Royal Marsden NHS Foundation Trust, we form the largest comprehensive cancer centre in Europe, dedicated to research that extends from epidemiology, genetics and molecular biology, through drug discovery and development, to cancer diagnosis and patient treatment. This makes us uniquely placed to work towards our vision that people may live their lives free from the fear of cancer as a life threatening disease. This Cancer Research UK Development Committee funded position will provide structural biology support for the hit-to-lead development of small molecule inhibitors of a protein kinase. The successful applicant will determine crystal structures of the kinase bound to small molecule inhibitors and contribute to the structure-based design of more potent, more specific inhibitors. The project will be carried out in the laboratory of Dr Richard Bayliss (Structural Biology), in collaboration with chemists at the Institute (Centre for Cancer Therapeutics), and the University of Newcastle. Applicants must hold a PhD, or be close to completing their PhD studies, in biochemistry, molecular biology or structural biology. An ability to independently determine X-ray crystal structures of proteins is essential. Experience in high-throughput crystallography for drug discovery would be considered an asset. The position is offered on a fixed term contract of up to two years in the first instance with a starting salary in the range £26,597 to £29,256 p.a. inclusive. Informal enquires may be made to Dr Richard Bayliss (Tel: +44 (0)20 7153 5557 / Email: [EMAIL PROTECTED]). Please DO NOT send your application to Dr Bayliss; CVs must be submitted in line with the instructions below. For further particulars and details of how to apply, please visit our website at www.icr.ac.uk. Alternatively you may call our 24 hour recruitment line on 020 7153 5475 quoting reference number C137. Closing date: 2 May 2008 The Institute of Cancer Research: Royal Cancer Hospital, a charitable Company Limited by Guarantee, Registered in England under Company No. 534147 with its Registered Office at 123 Old Brompton Road, London SW7 3RP. This e-mail message is confidential and for use by the addressee only. If the message is received by anyone other than the addressee, please return the message to the sender by replying to it and then delete the message from your computer and network.
[ccp4bb] Postdoc Vacancy at ICR, London
Post-doctoral Training Fellow - Structural Biology of Mitotic Regulation Section of Structural Biology, The Institute of Cancer Research, Chester Beatty Laboratories, Chelsea, London The Institute of Cancer Research (a College of the University of London) is a world-class cancer research organization with HEFCE RAE ratings of international excellence across all of its research programmes. In partnership with The Royal Marsden NHS Foundation Trust, we form the largest comprehensive cancer centre in Europe, dedicated to research that extends from epidemiology, genetics and molecular biology, through drug discovery and development, to cancer diagnosis and patient treatment. This makes us uniquely placed to work towards our vision that people may live their lives free from the fear of cancer as a life threatening disease. This Cancer Research UK funded position will investigate the structure and function of the Chfr protein (Checkpoint with Forkhead and RING domain), a ubiquitin E3 ligase and tumour suppressor involved in mitotic regulation. Chfr is crucial for a mitotic checkpoint that produces a cell-cycle delay in response to microtubule poisons. The successful applicant will determine crystal structures of Chfr bound to its protein partners and investigate the structural and cellular mechanisms of Chfr activity and regulation. The project is a collaboration between Dr Richard Bayliss (Structural Biology), Prof. Richard Marais (Cell and Molecular Biology) and Dr Spiros Linardopoulos (Breakthrough Breast Cancer). Applicants must hold a PhD, or be close to completing their PhD studies, in biochemistry, molecular biology or structural biology. Experience in molecular biology, protein expression and purification is essential. Experience in crystallographic structure determination using SAD/MAD/MIR techniques would be considered an asset. The position is offered on a fixed term contract of up to three years in the first instance with a starting salary in the range £26,597 to £31,551 p.a. inclusive. Informal enquires may be made to Dr Richard Bayliss (Tel: +44 (0)20 7153 5557 / Email: [EMAIL PROTECTED]). Please DO NOT send your application to Dr Bayliss; CVs must be submitted in line with the instructions below. For further particulars and details of how to apply, please visit our website at www.icr.ac.uk. Alternatively you may call our 24 hour recruitment line on 020 7153 5475 quoting reference number C128. Closing date: Friday 4th April 2008 The Institute of Cancer Research: Royal Cancer Hospital, a charitable Company Limited by Guarantee, Registered in England under Company No. 534147 with its Registered Office at 123 Old Brompton Road, London SW7 3RP. This e-mail message is confidential and for use by the addressee only. If the message is received by anyone other than the addressee, please return the message to the sender by replying to it and then delete the message from your computer and network.
