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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Published in: | Acta crystallographica. Section D, Biological crystallography. Vol. 58; no. 10-1; pp. 1560 - 1563 |
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Main Authors: | , , , , |
Format: | Journal Article |
Language: | English |
Published: |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
Munksgaard International Publishers
01-10-2002
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Subjects: | |
Online Access: | Get full text |
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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. |
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Bibliography: | ark:/67375/WNG-CR6W1ZCD-C istex:33C989DD51FB681AD38C341E855338AA8EE9805A 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 |