Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans

Chang Wei Wu; Lan Fen Li; Xiang Liu; Xiong Zhuo Gao; Jian Lei; Xiao Dong Su; Xiaojun Zhao; Yu He Liang

doi:10.2174/092986608784567519

Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans

Chang Wei Wu, Lan Fen Li, Xiang Liu, Xiong Zhuo Gao, Jian Lei, Xiao Dong Su, Xiaojun Zhao, Yu He Liang

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

Abstract

The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 Å. The crystal belonged to space group P2 ₁2₁2, with unit cell parameters a = 57.19 Å, b =94.76 Å, c =47.58 Å. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.

Original language	American English
Pages (from-to)	541-543
Number of pages	3
Journal	Protein and Peptide Letters
Volume	15
Issue number	5
DOIs	https://doi.org/10.2174/092986608784567519
State	Published - Jun 2008
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry

Keywords

Arginine biosynthesis
N-acetylglutamate kinase (NAGK)
Protein crystallography
Streptococcus mutans

Access to Document

10.2174/092986608784567519

Cite this

@article{064ac3987ca543989e907ee65379f255,

title = "Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans",

abstract = "The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 {\AA}. The crystal belonged to space group P2 1212, with unit cell parameters a = 57.19 {\AA}, b =94.76 {\AA}, c =47.58 {\AA}. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.",

keywords = "Arginine biosynthesis, N-acetylglutamate kinase (NAGK), Protein crystallography, Streptococcus mutans",

author = "Wu, {Chang Wei} and Li, {Lan Fen} and Xiang Liu and Gao, {Xiong Zhuo} and Jian Lei and Su, {Xiao Dong} and Xiaojun Zhao and Liang, {Yu He}",

year = "2008",

month = jun,

doi = "10.2174/092986608784567519",

language = "American English",

volume = "15",

pages = "541--543",

journal = "Protein and Peptide Letters",

issn = "0929-8665",

publisher = "Bentham Science Publishers",

number = "5",

}

TY - JOUR

T1 - Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans

AU - Wu, Chang Wei

AU - Li, Lan Fen

AU - Liu, Xiang

AU - Gao, Xiong Zhuo

AU - Lei, Jian

AU - Su, Xiao Dong

AU - Zhao, Xiaojun

AU - Liang, Yu He

PY - 2008/6

Y1 - 2008/6

N2 - The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 Å. The crystal belonged to space group P2 1212, with unit cell parameters a = 57.19 Å, b =94.76 Å, c =47.58 Å. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.

AB - The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 Å. The crystal belonged to space group P2 1212, with unit cell parameters a = 57.19 Å, b =94.76 Å, c =47.58 Å. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.

KW - Arginine biosynthesis

KW - N-acetylglutamate kinase (NAGK)

KW - Protein crystallography

KW - Streptococcus mutans

UR - http://www.scopus.com/inward/record.url?scp=45749157997&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=45749157997&partnerID=8YFLogxK

U2 - 10.2174/092986608784567519

DO - 10.2174/092986608784567519

M3 - Article

C2 - 18537747

SN - 0929-8665

VL - 15

SP - 541

EP - 543

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 5

ER -

Protein preparation, crystallization and preliminary X-ray crystallographic analysis of N-acetylglutamate kinase from Streptococcus mutans

Abstract

ASJC Scopus subject areas

Keywords

Access to Document

Other files and links

Fingerprint

Cite this