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14 June 2024 | Story Anthony Mthembu | Photo Suplied
Jeremiah Hlahla
Jeremiah Hlahla, a UFS student completing his PhD in Botany at the University of Debrecen as part of an exchange initiative funded by the Erasmus+ Mobility Programme.

As part of an exchange initiative facilitated by the Erasmus+ Mobility Programme, Jeremiah Hlahla, a student at the University of the Free State (UFS), is nearing the completion of his PhD studies at the University of Debrecen in Hungary. Hlahla’s  journey, which began in February 2024 and is set to conclude in July 2024, has been a remarkable learning opportunity. “As a first time-traveller to Europe, I have thoroughly enjoyed engaging with people from different countries and cultures,” he said.

The benefits of international collaboration

Hlahla is currently pursuing a PhD in Botany, focusing on plant stress physiology. “My current PhD project investigates the physiological, biochemical and morphological responses of vegetable-type soybean, or edamame, to combined drought and heat stress,’’ he explained. He considers the University of Debrecen the ideal institution to complete his research due to its extensive expertise and resources in similar projects. He noted that his colleagues at Debrecen conduct significant work on plant protection against biotic and abiotic stresses, including salt and drought stress, as well as proteins and amino acids in barley and other legumes.

Given the vast knowledge available on similar projects, Hlahla has found substantial engagement with his work at the University of Debrecen. “Upon arrival, I delivered an introductory lecture presenting my UFS project on the synergistic effects of combined drought and heat stress on the physiology and biochemistry of edamame. It was an engaging session as everyone could relate to my work and asked many questions,’’ he said.

Insights gained from the exchange

Hlahla has also gained valuable lessons that will assist him in his research career, including biotechnology and physiology tools. “I learned how to prepare samples and use high-performance liquid chromatography (HPLC) and reversed-phase ultra-high-performance liquid chromatography (UHPLC) to quantify proteins and amino acids,’’ he said. These techniques are beneficial not only for his current work but will also support future soybean research.   

As his experience at the University of Debrecen nears its end, Hlahla reflects on the collaborations and friendships he has formed, which stand out as a significant highlight.

News Archive

Chemistry postgraduates tackle crystallography with eminent international researcher
2017-04-04

Description: Dr Alice Brink  Tags: Dr Alice Brink

Department of Chemistry senior lecturer, Dr Alice Brink(left),
hosted outstanding researcher, Prof Elspeth Garman (right)
from the University of Oxford in England to present a
crystallography lecture.
Photo: Rulanzen Martin



“Crystallography forms part of everyday life.” This is according to Prof Elspeth Garman, eminent researcher from the Department of Biochemistry, University of Oxford in England, who was hosted by Dr Alice Brink, Department of Chemistry at the University of the Free State (UFS) Bloemfontein Campus. Prof Garman presented a lecture in the Department of Chemistry, titled ‘104 years of crystallography: What has it taught us and where will it lead’. She also taught the postgraduate students how to refine and mount protein structures in cold cryo conditions at about -173°C.

What is Crystallography?
Crystallography is the scientific technique which allows for the position of atoms to be determined in any matter which is crystalline.
 
“You cannot complete Protein Crystallography without the five key steps, namely obtaining a pure protein, growing the crystal, collecting the data, and finally determining the structure and atomic coordinates,” said Prof Garman. Apart from teaching, she was also here to mentor and have discussions with UFS Prestige Scholars on how to face academic challenges in the professional environment.

Discovery of the first crystal structure of a TB protein

Prof Garman successfully determined the first crystal structure of a Tuberculosis protein (TBNAT), a project that took about 15 years of research. In partnership with the Department of Pharmacology at Oxford University and an outstanding PhD student, Areej Abuhammad, they managed to grow only one TBNAT crystal, one-fiftieth of a millimetre. They also managed to solve the structure and publish it.

Dr Alice Brink, Senior Lecturer in the Department of Chemistry, says, “It’s an incredible privilege to have Prof Garman here and to have her share her wisdom and knowledge so freely with the young academics.”

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