Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus.

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Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus. / Drebes, Julia; Perbandt, Markus; Wrenger, Carsten; Betzel, Christian.

In: ACTA CRYSTALLOGR F, Vol. 67, No. Pt 4, Pt 4, 2011, p. 479-481.

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@article{630d087793284e27a71b262259de761b,
title = "Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus.",
abstract = "ThiM [5-(hydroxyethyl)-4-methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B(1) metabolism and has been crystallized by the vapour-diffusion method. The crystals belonged to the primitive space group P1, with unit-cell parameters a = 62.06, b = 62.40, c = 107.82?{\AA}, ? = 92.25, ? = 91.37, ? = 101.48° and six protomers in the unit cell, corresponding to a packing parameter V(M) of 2.3?{\AA}(3)?Da(-1). Diffraction data were collected to 2.1?{\AA} resolution using synchrotron radiation. The phase problem was solved by molecular replacement.",
keywords = "Crystallography, X-Ray, Crystallization, Phosphotransferases (Alcohol Group Acceptor)/*chemistry/isolation & purification, Staphylococcus aureus/*enzymology, Crystallography, X-Ray, Crystallization, Phosphotransferases (Alcohol Group Acceptor)/*chemistry/isolation & purification, Staphylococcus aureus/*enzymology",
author = "Julia Drebes and Markus Perbandt and Carsten Wrenger and Christian Betzel",
year = "2011",
language = "English",
volume = "67",
pages = "479--481",
journal = "ACTA CRYSTALLOGR F",
issn = "2053-230X",
publisher = "John Wiley and Sons Ltd",
number = "Pt 4",

}

RIS

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus.

AU - Drebes, Julia

AU - Perbandt, Markus

AU - Wrenger, Carsten

AU - Betzel, Christian

PY - 2011

Y1 - 2011

N2 - ThiM [5-(hydroxyethyl)-4-methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B(1) metabolism and has been crystallized by the vapour-diffusion method. The crystals belonged to the primitive space group P1, with unit-cell parameters a = 62.06, b = 62.40, c = 107.82?Å, ? = 92.25, ? = 91.37, ? = 101.48° and six protomers in the unit cell, corresponding to a packing parameter V(M) of 2.3?Å(3)?Da(-1). Diffraction data were collected to 2.1?Å resolution using synchrotron radiation. The phase problem was solved by molecular replacement.

AB - ThiM [5-(hydroxyethyl)-4-methylthiazole kinase; EC 2.7.1.50] from Staphylococcus aureus is an essential enzyme of thiamine or vitamin B(1) metabolism and has been crystallized by the vapour-diffusion method. The crystals belonged to the primitive space group P1, with unit-cell parameters a = 62.06, b = 62.40, c = 107.82?Å, ? = 92.25, ? = 91.37, ? = 101.48° and six protomers in the unit cell, corresponding to a packing parameter V(M) of 2.3?Å(3)?Da(-1). Diffraction data were collected to 2.1?Å resolution using synchrotron radiation. The phase problem was solved by molecular replacement.

KW - Crystallography, X-Ray

KW - Crystallization

KW - Phosphotransferases (Alcohol Group Acceptor)/chemistry/isolation & purification

KW - Staphylococcus aureus/enzymology

KW - Crystallography, X-Ray

KW - Crystallization

KW - Phosphotransferases (Alcohol Group Acceptor)/chemistry/isolation & purification

KW - Staphylococcus aureus/enzymology

M3 - SCORING: Journal article

VL - 67

SP - 479

EP - 481

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - Pt 4

M1 - Pt 4

ER -