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Purification, crystallization and preliminary X-ray diffraction analysis of human oncoprotein SET/TAF-1beta
Shinsuke Muto1, Miki Senda, Naruhiko Adachi
1Horikoshi Gene Selector Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), 5-9-6 Tokodai, Tsukuba, Ibaraki 300-2635, Japan.
Summary
The human oncoprotein SET/TAF-1beta was successfully crystallized using ammonium sulfate. This structural study provides insights into the protein
Area of Science:
- Structural biology
- Protein crystallography
- Biochemistry
Background:
- The human oncoprotein SET/TAF-1beta plays a role in cellular processes.
- Understanding its structure is crucial for comprehending its function.
Purpose of the Study:
- To determine the crystal structure of the human oncoprotein SET/TAF-1beta.
- To facilitate further functional and mechanistic studies.
Main Methods:
- Crystallization was achieved using the sitting-drop vapor-diffusion method.
- Ammonium sulfate was employed as a precipitant.
- X-ray diffraction data were collected to 2.8 A resolution using synchrotron radiation.
Main Results:
- The crystal belongs to space group C2.
- Unit-cell parameters: a = 119.6, b = 62.8, c = 61.0 A, beta = 89.7 degrees.
- Two molecules of SET/TAF-1beta were found in the asymmetric unit.
Conclusions:
- The successful crystallization and data collection pave the way for detailed structural analysis.
- This structural information will aid in understanding the role of SET/TAF-1beta in oncogenesis.