Literature DB >> 16552135

The structure of the hexagonal crystal form of hen egg-white lysozyme.

C Brinkmann1, M S Weiss, E Weckert.   

Abstract

The three-dimensional structure of hen egg-white lysozyme (HEWL) in a hexagonal crystal form has been determined and refined to 1.46 A resolution. This hexagonal crystal form crystallizes from a saturated sodium nitrate solution at pH 8.4. The crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. A total of 165 water molecules, 16 nitrate ions and five sodium ions were located in the electron-density map. The hexagonal crystal form exhibits a higher solvent content and a higher degree of disorder than other crystal forms of lysozyme. The flexibility of the protein depends on the crystal packing, although some residue ranges are flexible in all native HEWL crystal forms.

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Year:  2006        PMID: 16552135     DOI: 10.1107/S0907444906000825

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  5 in total

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4.  The potential of hexatungstotellurate(VI) to induce a significant entropic gain during protein crystallization.

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Journal:  IUCrJ       Date:  2017-10-27       Impact factor: 4.769

5.  Localization and orientation of heavy-atom cluster compounds in protein crystals using molecular replacement.

Authors:  Sven O Dahms; Miriam Kuester; Carsten Streb; Christian Roth; Norbert Sträter; Manuel E Than
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2013-01-19
  5 in total

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