Crystallization and preliminary diffraction analysis of the HincII restriction endonuclease-DNA complex

Nancy C Horton, Lydia F. Dorner, Ira Schildkraut, John J. Perona

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Crystals of the 60 kDa dimeric HincII restriction enzyme bound to a 12 base-pair dyad-symmetric duplex DNA carrying the specific 5'-GTCGAC recognition site have been obtained. Crystals grew by hanging-drop vapor diffusion from solutions containing polyethylene glycol 4000 as precipitating agent. The rod-shaped crystals belong to space group I222 (or I212121), with unit-cell dimensions a = 66.9, b = 176.7, c = 256.0 Å. There are most likely to be two dimeric complexes in the asymmetric unit. A complete native data set has been collected from a high-energy synchrotron source to a resolution of 2.5 Å at 100 K, with an R(merge) of 4.8%.

Original languageEnglish (US)
Pages (from-to)1943-1945
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number11
DOIs
StatePublished - Nov 1999
Externally publishedYes

Fingerprint

Synchrotrons
DNA Restriction Enzymes
Crystallization
Base Pairing
constrictions
deoxyribonucleic acid
Diffraction
crystallization
Crystals
DNA
Enzymes
diffraction
crystals
enzymes
glycols
polyethylenes
synchrotrons
rods
Vapors
vapors

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Crystallization and preliminary diffraction analysis of the HincII restriction endonuclease-DNA complex. / Horton, Nancy C; Dorner, Lydia F.; Schildkraut, Ira; Perona, John J.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 11, 11.1999, p. 1943-1945.

Research output: Contribution to journalArticle

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