be exchanged and made freely available
X-ray diffraction data using ice-binding protein (LeIBP) crystal
Psychrophilic Arctic yeast Leucosporidium sp. produces a glycosylated ice-binding protein (LeIBP) with a molecular mass of approximately 25 kDa, which can lower the freezing point below the melting point once it binds to ice. LeIBP exhibits low amino acid sequence similarity to other antifreeze proteins with known protein structures. Recently, we developed an expression system allowing high-level production and efficient purification of recombinant pLeIBP. Furthermore, crystallization and preliminary X-ray crystallographic analysis of the ice-binding protein were performed. To investigate the antifreeze mechanism of LeIBP, we have carried out structural studies. As the first step toward its structural elucidation, we report the results of preliminary X-ray crystallographic experiments with LeIBP.
- Entry ID
- KOPRI-KPDC-00000230
- KPDC_X-ray_LeIBP_2012 (Old ID)
- Copyright
- Science Keyword
- ISO Topic
- BIOTA
- Platforms
- X-ray diffraction(X-ray diffraction)
- Instruments
- Rigaku micromax-007 HF( Korea Basic Science Institute, Using Rigaku micromax-007 HF model's X-ray diffraction analysis equipment)
- Mark II Coring system
- Personnel
- Jun Hyuck Lee (junhyucklee@kopri.re.kr)
- Create/Update Date
- 2012-06-26 / 2012-06-26
- Citation
- The data(KOPRI-KPDC-00000230) used in this work was provided by the Korea Polar Research Institute.