Crystallization of the gene 45 protein from the DNA replication fork of bacteriophage T4

C. Thaller; B. Alberts; E. Goldsmith; S. Sprang; R. Fletterick

Crystallization of the gene 45 protein from the DNA replication fork of bacteriophage T4

C. Thaller, B. Alberts, E. Goldsmith, S. Sprang, R. Fletterick

Research output: Contribution to journal › Article › peer-review

Abstract

The gene 45 protein from bacteriophage T4 has been purified and is crystallized. This protein is part of the T4 DNA replication complex. The crystallized protein is active in complementation assays. X-ray diffraction analysis is in progress; data are measured for the native and several heavy atom derivatives. The crystals diffract to about 3.5-Å resolution.

Original language	English (US)
Pages (from-to)	2568-2569
Number of pages	2
Journal	Journal of Biological Chemistry
Volume	259
Issue number	4
State	Published - 1984

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Cite this

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title = "Crystallization of the gene 45 protein from the DNA replication fork of bacteriophage T4",

abstract = "The gene 45 protein from bacteriophage T4 has been purified and is crystallized. This protein is part of the T4 DNA replication complex. The crystallized protein is active in complementation assays. X-ray diffraction analysis is in progress; data are measured for the native and several heavy atom derivatives. The crystals diffract to about 3.5-{\AA} resolution.",

author = "C. Thaller and B. Alberts and E. Goldsmith and S. Sprang and R. Fletterick",

year = "1984",

language = "English (US)",

volume = "259",

pages = "2568--2569",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "4",

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T1 - Crystallization of the gene 45 protein from the DNA replication fork of bacteriophage T4

AU - Thaller, C.

AU - Alberts, B.

AU - Goldsmith, E.

AU - Sprang, S.

AU - Fletterick, R.

PY - 1984

Y1 - 1984

N2 - The gene 45 protein from bacteriophage T4 has been purified and is crystallized. This protein is part of the T4 DNA replication complex. The crystallized protein is active in complementation assays. X-ray diffraction analysis is in progress; data are measured for the native and several heavy atom derivatives. The crystals diffract to about 3.5-Å resolution.

AB - The gene 45 protein from bacteriophage T4 has been purified and is crystallized. This protein is part of the T4 DNA replication complex. The crystallized protein is active in complementation assays. X-ray diffraction analysis is in progress; data are measured for the native and several heavy atom derivatives. The crystals diffract to about 3.5-Å resolution.

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AN - SCOPUS:0021362874

SN - 0021-9258

VL - 259

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 4

ER -

Crystallization of the gene 45 protein from the DNA replication fork of bacteriophage T4

Abstract

ASJC Scopus subject areas

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