Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8

Yuichi Taguchi, Jun Hoseki, Yoshimitsu Kakuta, Keiichi Fukuyama

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

ATP sulfurylase catalyzes the reaction of inorganic sulfate with ATP, producing adenosine-5′-phosphosulfate (APS) and pyrophosphate. A probable ATP sulfurylase (MW = 38.8 kDa) from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. It was crystallized in the presence of 5 mM APS by the batch method. The crystal was monoclinic, space group P2 1, with unit-cell parameters a = 68.8, b = 61.2, c = 128.6 Å, β = 95.4°. Diffraction to better than 2.5 Å resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (VM = 3.48 Å3 Da -1).

Original languageEnglish
Pages (from-to)1645-1647
Number of pages3
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number9
DOIs
Publication statusPublished - Sep 1 2003

Fingerprint

Sulfate Adenylyltransferase
Adenosine Phosphosulfate
Thermus thermophilus
adenosine triphosphate
Crystallization
X-Ray Diffraction
X ray diffraction analysis
adenosines
crystallization
Synchrotrons
Synchrotron radiation
diffraction
Adenosine Diphosphate
Escherichia coli
Sulfates
x rays
Adenosine Triphosphate
Diffraction
Radiation
Escherichia

All Science Journal Classification (ASJC) codes

  • Structural Biology

Cite this

Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8. / Taguchi, Yuichi; Hoseki, Jun; Kakuta, Yoshimitsu; Fukuyama, Keiichi.

In: Acta Crystallographica - Section D Biological Crystallography, Vol. 59, No. 9, 01.09.2003, p. 1645-1647.

Research output: Contribution to journalArticle

@article{3120b8a89bc941d4832f4c5bf68abe50,
title = "Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8",
abstract = "ATP sulfurylase catalyzes the reaction of inorganic sulfate with ATP, producing adenosine-5′-phosphosulfate (APS) and pyrophosphate. A probable ATP sulfurylase (MW = 38.8 kDa) from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. It was crystallized in the presence of 5 mM APS by the batch method. The crystal was monoclinic, space group P2 1, with unit-cell parameters a = 68.8, b = 61.2, c = 128.6 {\AA}, β = 95.4°. Diffraction to better than 2.5 {\AA} resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (VM = 3.48 {\AA}3 Da -1).",
author = "Yuichi Taguchi and Jun Hoseki and Yoshimitsu Kakuta and Keiichi Fukuyama",
year = "2003",
month = "9",
day = "1",
doi = "10.1107/S0907444903014641",
language = "English",
volume = "59",
pages = "1645--1647",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "9",

}

TY - JOUR

T1 - Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8

AU - Taguchi, Yuichi

AU - Hoseki, Jun

AU - Kakuta, Yoshimitsu

AU - Fukuyama, Keiichi

PY - 2003/9/1

Y1 - 2003/9/1

N2 - ATP sulfurylase catalyzes the reaction of inorganic sulfate with ATP, producing adenosine-5′-phosphosulfate (APS) and pyrophosphate. A probable ATP sulfurylase (MW = 38.8 kDa) from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. It was crystallized in the presence of 5 mM APS by the batch method. The crystal was monoclinic, space group P2 1, with unit-cell parameters a = 68.8, b = 61.2, c = 128.6 Å, β = 95.4°. Diffraction to better than 2.5 Å resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (VM = 3.48 Å3 Da -1).

AB - ATP sulfurylase catalyzes the reaction of inorganic sulfate with ATP, producing adenosine-5′-phosphosulfate (APS) and pyrophosphate. A probable ATP sulfurylase (MW = 38.8 kDa) from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. It was crystallized in the presence of 5 mM APS by the batch method. The crystal was monoclinic, space group P2 1, with unit-cell parameters a = 68.8, b = 61.2, c = 128.6 Å, β = 95.4°. Diffraction to better than 2.5 Å resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (VM = 3.48 Å3 Da -1).

UR - http://www.scopus.com/inward/record.url?scp=0042285513&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0042285513&partnerID=8YFLogxK

U2 - 10.1107/S0907444903014641

DO - 10.1107/S0907444903014641

M3 - Article

C2 - 12925800

AN - SCOPUS:0042285513

VL - 59

SP - 1645

EP - 1647

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 9

ER -