Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C

Peter H. Rehse, Yuichi Nodake, Chizu Kuroishi, Tahir H. Tahirov

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Selenium-incorporated osmotically inducible protein C from the thermophilic bacterium Thermus thermophilus was overexpressed, purified and crystallized. The crystals belong to space group P1, with unit-cell parameters a = 37.58, b = 40.95, c = 48.14 Å, α = 76.93, β = 74.04, γ = 64.05°. Five data sets were collected from a single crystal to 1.6 Å using synchrotron radiation for MAD phasing. Self-rotation functions and the Matthews coefficient are consistent with two molecules in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)357-358
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number2
DOIs
StatePublished - Feb 1 2004

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Thermus thermophilus
Synchrotrons
Selenium
Crystallization
Protein C
selenium
Synchrotron radiation
purification
bacteria
Purification
Bacteria
synchrotron radiation
Single crystals
Radiation
crystallization
proteins
Crystals
Molecules
single crystals
coefficients

ASJC Scopus subject areas

  • Structural Biology

Cite this

Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C. / Rehse, Peter H.; Nodake, Yuichi; Kuroishi, Chizu; Tahirov, Tahir H.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, No. 2, 01.02.2004, p. 357-358.

Research output: Contribution to journalArticle

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