Halina Mikolajek


Halina Mikolajek is a Senior Support Scientist working for VMXi and the Crystallisation Facility Manager within the Research Complex at Harwell. Before joining Diamond in 2017, she was a Postdoc at the University of Southampton.

Email: halina.mikolajek@diamond.ac.uk
Tel: +44 (0) 1235 778161

Key Research Area

Other Specialist Areas

  • Beamline Development

Latest Publications

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  1. Research Expertise
  2. Publications
Research Expertise -

Current Research Interests

My current role is to organise and manage the crystallisation facility within the Research Complex at Harwell/Diamond and support users of the VMXi beamline. This beamline will operate entirely automatically, collecting X-ray diffraction data from macromolecular crystals in situ (in the tray in which they were grown).

I am working on new crystallisation methods in conjunction with James Sandy and Juan Sanchez Weatherby. 



Publications - +
  1. Papakyria, A. et al. The partial dissociation of MHC class I bound peptides exposes their N terminus to trimming by endoplasmic reticulum aminopeptidase 1. J. Biol. Chem. DOI:10.1074/JBC.RA117.000313 (2018)
  2. Moore, C. E. et al. Elongation Factor 2 Kinase is Regulated by Proline Hydroxylation and Protects Cells during Hypoxia. Mol Cell Biol. 35, 1788-1804, DOI: 10.1128/MCB.01457-14 (2015)
  3. Xie, J. et al. Molecular Mechanism for the Control of Eukaryotic Elongation Factor 2 Kinase by pH: Role in Cancer Cell Survival. Mol Cell Biol. 35, 1805-1824, DOI: 10.1128/MCB.00012-15 (2015)
  4. Becker, A.K. et al. Characterisation of recobinantly expressed matrilin VWA domains. Protein Exp Purif. 107, 20-28, DOI:10.1016/j.pep.2014.11.005 (2015)
  5. Becker, A.K. et al. A structure of a collagen VI VMW domain displays N and C termini at opposite sides of the protein. Structure 22, 199-208, DOI: 10.1016/j.str.2013.06.028 (2014)
  6. Moore, C.E. et al. A conserved loop in the catalytic domain of eukaryotic elongation factor 2 kinase plays a key role in its substrate specificity. Mol. Cell Biol. 34, 2294-2307, DOI: 10.1128/MCB.00388-14 (2014)
  7. Phippen, C.W. et al. Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginose MorA, a bi-functional c-di-GMP regulator. FEBS Letter. 588, 4631-4636, DOI: 10.1016/j.febslet.2014.11.002 (2014)
  8. Smith, K. M. et al. 2β-deoxy-Kdo is an inhibitor of the Arabidopsis thaliana CMP-2-Keto-3-deoxymanno-octulosonic acid synthetase, the enzyme required for activation of Kdo prior to incorporation into rhamnogalacturonan II. Mol. Plant. 6, 981-984, DOI: 10.1093/mp/sst011 (2013)
  9. Roberts, A. et al. Insights into the mechanism of pyrrole polymerization catalysed by porphobilinogen deaminase: high resolution X-ray analysis X-ray studies of the Arabidopsis thaliana enzyme. Acta Crystallographica Section F 68, 471-485 DOI: 10.1107/S0907444912052134 (2013)
  10. Roberts, A. et al. Crystallisation and preliminary X-ray characterisation of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana. Acta Crystallographica. Section F 68, 1491-1493, DOI: 10.1107/S1744309112042212 (2012)
  11. Pigott, C.R. et al. Insights into the regulation of eukaryotic elongation factor 2 kinase and the interplay between its domains. Biochem. J. 442, 105-118, DOI: 10.1042/BJ20111536 (2012)
  12. Mikolajek, H. et al. Structural basis of ligand binding specificity in the human pentraxins, C-reactive protein and serum amyloid P component. J. Mol. Recognition 24, 125-136, DOI: 10.1002/jmr.1090 (2011)
  13. Bowyer, A. et al. Structure and function of the l-threonine dehydrogenase (TkTDH) from the thermophilic arcjaeon Thermococccus kodakaraensis. J. Struct. Biol. 168, 294-304, DOI: 10.1016/j.jsb.2009.07.011 (2009)
  14. Bowyer, A. et al. Crystallization and preliminary X-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis. Acta Crystallographica. Section F, Biological crystallography 64, 828-830, DOI: 10.1107/S1744309108025384 (2008)
  15. Erskine, P.T. et al. High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei. J. Mol. Biol. 363, 125-136, DOI: 10.1016/j.jmb.2006.07.069 (2006)
  16. Knight, M.J. et al. Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei. Acta crystallographica. Section F 62, 761-764, DOI: 10.1107/S1744309106024857 (2006).