Abstract

HutP is an RNA-binding protein and regulates the expression of the histidine utilization ( hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on hut mRNA. HutP and its mutant, which has increased affinity for the regulatory sequences, were purified and crystallized by the hanging-drop vapor diffusion method. The space group was P2 13 with unit cell dimensions a=b=c=95.6 A ̊ for HutP and a=b=c=96.8 A ̊ for the mutant. Complete data sets of 3.0-Å resolution for wild-type HutP and of 2.70-Å resolution for the mutant HutP were collected.

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