The Douglas OryXNano crystallization robot provides the opportunity of screening a great range of crystallization conditions saving time and sample quantity. Oryx system uses multi-bore dispensing tips (microtips), which have several independent channels to dispense small volumes. At the end of a 3-bore tip there are three holes. Each channel dispenses a different solution. The solutions do not mix in the tip - they mix in the drop after they are dispensed. This means that there is no dead-volume.The microtip always touches the plate when liquids are dispensed. This gives very reliable dispensing. Stock solutions do not come into contact with the motorized syringes, which are filled with degassed pure water - this avoids the need for flushing out the syringes when the stock solutions are changed.The manual syringes on the front panel are used to refill the motorized syringes, to remove air bubbles, and to load stock solutions for optimization experiments.Screening for sitting drop is carried out using plates that are prefilled with reservoir solutions. (Reservoirs can be filled manually with a 12-channel pipette. A very simple user-interface is used to design experiments, as shown below. The correct plate can be selected from a database of all well-known crystallization plates (if your favorite isn't there, let us know!), the volumes of each ingredient of a drop are entered in a simple form. Individual wells can be selected or skipped by clicking on the plate with a mouse.
EDUCATION
2019: PhD in Structural Biology and Protein Biomaterials (UoC, IMBB-FORTH - Greece)
2012: M.Sc. in Protein Biotechnology (UoC-Greece)
2009: Diploma Degree in Biology (UoC-Greece)
WORKING EXPERIENCE
Oct 2019 – Now: Post-Doctoral Researcher at I.M.B.B.-F.O.R.TH, Greece
(Laboratory of Structural Biology)
Sep 2020 – Now: Autonomous teaching and exam organizing of the under-graduate courses
"Enzymatic Biotechnology" and “Protein Engineering” at the Dept. of
Biology of the Uni. of Crete
2014 – 2020: Experienced scientist position at I.M.B.B.-F.O.R.TH, Greece (InnovCrete project /FP7-Regpot program) and at University of Crete
Oct. 2010 –Jan. 2011: Laboratory Teaching Assistant of Microbiology Teaching Lab
at the Dept. of Biology, Uni. of Crete
SELECTED PUBLICATIONS
*Kefala K., Kotsifaki D., Providaki M., Kapetaniou E., Rahme L. and Kokkinidis M. Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein of Pseudomonas aeruginosa. (2012). Acta. Cryst F, 68, 695-697
*Kefala A., Kotsifaki D., Providaki M., Amprazi M. and Kokkinidis M. Expression, purification and crystallization of a protein resulting from the inversion of the aminoacid sequence of a helical bundle. (2017). ). Acta. Cryst F, 73, 51-53
Dimovasili C., Fadouloglou V.E., Kefala A., Providaki M., Kotsifaki D, Sarrou I., Plaitakis A., Zaganas I. and Kokkinidis M. Crystal structure of glutamate dehydrogenase 2, a positively selected novel human enzyme involved in brain biology and cancer pathophysiology. Journal of Neurochemistry (accepted)
RESEARCH PROFILE
Being in a Structural Biology group since 2011, Dr. Kefala A. has studied deeply the protein folding problem, elucidating the relation between amino acid sequence and structural properties of α-helical bundles. The knowledge obtained was used for protein design leading to bio-derived materials for bio-medical applications and basic research through structural studies of protein folding through reverse sequences.
Notable achievements include:
The elucidation of the protein folding of mutants of the α-helical protein Rop that is used as a canonical paradigm of this structural motif.
Protein design of novel protein-based biomaterials with specific engineered properties.