Literature DB >> 2060631

Growth inhibition of lysozyme crystals at high hydrostatic pressure.

M Gross1, R Jaenicke.   

Abstract

The influence of high hydrostatic pressures on the crystallization of hen egg-white lysozyme has been determined by growing lysozyme crystals with a capillary technique adapted to high pressure conditions and monitoring the residual protein concentration remaining in the supernatant. Pressure is found to reduce the rate of crystallization and to enhance the solubility of lysozyme in 1 M NaCl, pH 4.66. The volume change calculated from the latter result amounts to 12.5 ml/mol. This value is too small to be detectable by comparison of total molar volumes.

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Year:  1991        PMID: 2060631     DOI: 10.1016/0014-5793(91)80768-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  The effect of ionic strength, temperature, and pressure on the interaction potential of dense protein solutions: from nonlinear pressure response to protein crystallization.

Authors:  Johannes Möller; Martin A Schroer; Mirko Erlkamp; Sebastian Grobelny; Michael Paulus; Sebastian Tiemeyer; Florian J Wirkert; Metin Tolan; Roland Winter
Journal:  Biophys J       Date:  2012-06-05       Impact factor: 4.033

  1 in total

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