Crystallization and preliminary X-ray analysis of catalase–peroxidase from the halophilic archaeon<i>Haloarcula marismortui</i>

Yusuke Yamada, Shinya Saijo, Takao Sato, Noriyuki Igarashi, Hideo Usui, Taketomo Fujiwara, Nobuo Tanaka

Acta Crystallographica Section D Biological Crystallography · 2001 · 14 citations · 4 references

Concepts

Abstract

Catalase-peroxidases are bifunctional enzymes found in many microorganisms. Crystals of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui were obtained using the hanging-drop vapour-diffusion method. The rhombic plate-shaped crystals were grown from purified protein solution using (NH(4))(2)SO(4) as precipitant at 293 K. The crystal belongs to the monoclinic system, space group C2, and diffracted beyond 2.0 A resolution.

References

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