Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT‐3. Issue 7 (22nd July 2013)

• Record Type: Journal Article
• Authors: Zárate‐Romero, Andrés; Stojanoff, Vivian; Rojas‐Trejo, Sonia Patricia; Hansberg, Wilhelm; Rudiño‐Piñera, Enrique
• Is Part Of: Acta crystallographica. Volume 69:Issue 7(2013:Jul.)
• Page Start: 753
• Page End: 758
• Publication Date: 2013-07-22
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113013468
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Polymorphism is frequently observed from different crystallization conditions. In proteins, the effect on conformational variability is poorly documented, with only a few reported examples. Here, three polymorphic crystal structures determined for a large‐subunit catalase, CAT‐3 from <italic>Neurospora crassa</italic>, are reported. Two of them belonged to new space groups, <italic>P</italic>1 and <italic>P</italic>4₃2₁2, and a third structure belonged to the same space group, <italic>P</italic>2₁2₁2₁, as the previously deposited 2.3 Å resolution structure (PDB entry 3ej6), but had a higher resolution (1.95 Å). Comparisons between these polymorphic structures highlight the conformational stability of tetrameric CAT‐3 and reveal a distortion in the tetrameric structure that has not previously been described.</p> </abstract>