Comparison of two crystal polymorphs of NowGFP reveals a new conformational state trapped by crystal packing.

ABSTRACT: Crystal polymorphism serves as a strategy to study the conformational flexibility of proteins. However, the relationship between protein crystal packing and protein conformation often remains elusive. In this study, two distinct crystal forms of a green fluorescent protein variant, NowGFP, are compared: a previously identified monoclinic form (space group C2) and a newly discovered orthorhombic form (space group P2₁2₁2₁). Comparative analysis reveals that both crystal forms exhibit nearly identical linear assemblies of NowGFP molecules interconnected through similar crystal contacts. However, a notable difference lies in the stacking of these assemblies: parallel in the monoclinic form and perpendicular in the orthorhombic form. This distinct mode of stacki

SUBMITTER: Kim JK 

PROVIDER: S-EPMC11394120 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature