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

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

doi:10.1107/S0907444999010574

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 journal › Article › peer-review

7 Scopus citations

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 language	English (US)
Pages (from-to)	1943-1945
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
Issue number	11
DOIs	https://doi.org/10.1107/S0907444999010574
State	Published - Nov 1999

ASJC Scopus subject areas

Structural Biology

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title = "Crystallization and preliminary diffraction analysis of the HincII restriction endonuclease-DNA complex",

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 {\AA}. 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 {\AA} at 100 K, with an R(merge) of 4.8%.",

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T1 - Crystallization and preliminary diffraction analysis of the HincII restriction endonuclease-DNA complex

AU - Horton, Nancy C.

AU - Dorner, Lydia F.

AU - Schildkraut, Ira

AU - Perona, John J.

PY - 1999/11

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AB - 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%.

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

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