Crystallization and preliminary X-ray analysis of methionine aminopeptidase from the hyperthermophilic bacterium Pyrococcus furiosus

Tahir H. Tahirov, Hideyuki Oki, Tomitake Tsukihara, Kyoko Ogasahara, Yukiko Izu, Susumu Tsunasawa, Ikunoshin Kato, Katsuhide Yutani

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Methionine aminopeptidase (MAP) from Pyrococcus furiosus (Pfu) has been crystallized in four different forms (A, B, C and D). Form A crystals belong to space group P21 with unit-cell dimensions a = 54.18, b = 85.72, c = 72.84 Å, β = 108.34°. Forms B, C and D belong to space group P6(2(4)) with unit-cell dimensions a = 139.1, c = 63.7 Å for form B, a = 198.6, c = 243.8 Å for form C, and a= 111.0, c = 125.0 Å for form D. Forms A and D diffract to 2.9 Å, form B diffracts to 3.5 Å, and form C crystals diffract to 4.5 A. Form Å contains two molecules of MAP-Pfu per asymmetric unit. The binuclear metal center positions and a non-crystallographic twofold symmetry matrix has been determined for the form A crystals.

Original languageEnglish (US)
Pages (from-to)798-801
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume53
Issue number6
DOIs
StatePublished - Jan 1 1997

    Fingerprint

ASJC Scopus subject areas

  • Structural Biology

Cite this