Understanding the polymorphic behaviour of a mutant of the -spectrin SH3 domain by means of two 1.1 Å resolution structures

Ana Cámara-Artigas, Jose Antonio Gavira, Salvador Casares, Juan Manuel Garcia-Ruiz, Francisco Conejero-Lara, James Allen, Jose C. Martinez

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


SH3 domains are small protein modules that mediate the assembly of specific protein complexes, typically via binding to proline-rich sequences in their respective binding partners. Most of the -spectrin SH3-domain (Spc-SH3) structures determined to date using X-ray diffraction have been solved from crystals belonging to the orthorhombic space group P212121 with a needle-like morphology. All of these ortho-rhombic crystals exhibited a rapid growth rate. In addition to this crystal form, the R21D mutant of Spc-SH3 crystallizes in a new crystal form in the presence of sodium formate at pH values higher than 6. This new crystal form grows at a slower rate and belongs to the hexagonal space group P6522, with unit-cell parameters a = b = 42.9, c = 127.5 Å. When both polymorphs of the R21D mutant of Spc-SH3 are simultaneously present into the same solution, it has been observed that the hexagonal crystals grow at the expense of the orthorhombic crystals. The availability of 1.1 Å resolution structures for both crystal forms allows the identification of key features that could account for the observed polymorphic behaviour.

Original languageEnglish (US)
Pages (from-to)189-196
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Issue number3
StatePublished - Mar 1 2011


  • Ostwalds rule
  • SH3 domains
  • polymorphism

ASJC Scopus subject areas

  • Structural Biology


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