4bim

Publication Abstract from PubMed

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 Neurospora crassa, are reported. Two of them belonged to new space groups, P1 and P43212, and a third structure belonged to the same space group, P212121, as the previously deposited 2.3 A resolution structure (PDB entry 3ej6), but had a higher resolution (1.95 A). 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.

Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3.,Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul 1;69(Pt 7):753-8. doi:, 10.1107/S1744309113013468. Epub 2013 Jun 27. PMID:23832201^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.