BPTI liquid-liquid phase separation monitored by light and small angle X-ray scattering

In the field of protein crystallization, a better knowledge of the nucleation process is essential to control the nucleation rate, the growth and therefore the size and the quality of crystals. With that aim, it becomes clear that the important stage is the determination of the protein phase diagram...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Vol. 58; no. 10-1; pp. 1560 - 1563
Main Authors: Grouazel, S., Perez, J., Astier, J.-P., Bonneté, F., Veesler, S.
Format: Journal Article
Language:English
Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01-10-2002
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Summary:In the field of protein crystallization, a better knowledge of the nucleation process is essential to control the nucleation rate, the growth and therefore the size and the quality of crystals. With that aim, it becomes clear that the important stage is the determination of the protein phase diagram. We highlighted and investigated the bovine pancreatic trypsin inhibitor (BPTI) binary liquid‐liquid phase separation in 350 mM KSCN solutions as a function of temperature. We measured the low concentration part of the binodal curve using light scattering and optical microscopy. We show, from small angle X‐ray scattering experiments, that the high concentrated phase sediments in the bottom of the capillary and we analysed the low concentrated phase in terms of monomers/decamers equilibrium.
Bibliography:ark:/67375/WNG-CR6W1ZCD-C
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ArticleID:AYDIC0041
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902012799