Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans

Research output: Contribution to journalJournal articleResearchpeer-review

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Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans. / Cao, Yan Li; Li, Gui Lan; Wang, Kai Tuo; Zhang, Hong Yin; Li, Lan Fen.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 6, 01.06.2011, p. 682-684.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Cao, YL, Li, GL, Wang, KT, Zhang, HY & Li, LF 2011, 'Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 67, no. 6, pp. 682-684. https://doi.org/10.1107/S1744309111011377

APA

Cao, Y. L., Li, G. L., Wang, K. T., Zhang, H. Y., & Li, L. F. (2011). Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(6), 682-684. https://doi.org/10.1107/S1744309111011377

Vancouver

Cao YL, Li GL, Wang KT, Zhang HY, Li LF. Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2011 Jun 1;67(6):682-684. https://doi.org/10.1107/S1744309111011377

Author

Cao, Yan Li ; Li, Gui Lan ; Wang, Kai Tuo ; Zhang, Hong Yin ; Li, Lan Fen. / Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2011 ; Vol. 67, No. 6. pp. 682-684.

Bibtex

@article{d85a271978bb4f538cd955aa82357847,
title = "Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans",
abstract = "Argininosuccinate lyase (ASL) is an important enzyme in arginine synthesis and the urea cycle, which are highly conserved from bacteria to eukaryotes. The gene encoding Streptococcus mutans ASL (smASL) was amplified and cloned into expression vector pET28a. The recombinant smASL protein was expressed in a soluble form in Escherichia coli strain BL21 (DE3) and purified to homogeneity by two-step column chromatography. Crystals suitable for X-ray analysis were obtained and X-ray diffraction data were collected to a resolution of 2.5 {\AA}. The crystals belonged to space group R3, with unit-cell parameters a = b = 254.5, c = 78.3 {\AA}.",
keywords = "argininosuccinate lyase, Streptococcus mutans",
author = "Cao, {Yan Li} and Li, {Gui Lan} and Wang, {Kai Tuo} and Zhang, {Hong Yin} and Li, {Lan Fen}",
year = "2011",
month = jun,
day = "1",
doi = "10.1107/S1744309111011377",
language = "English",
volume = "67",
pages = "682--684",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "6",

}

RIS

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of argininosuccinate lyase from Streptococcus mutans

AU - Cao, Yan Li

AU - Li, Gui Lan

AU - Wang, Kai Tuo

AU - Zhang, Hong Yin

AU - Li, Lan Fen

PY - 2011/6/1

Y1 - 2011/6/1

N2 - Argininosuccinate lyase (ASL) is an important enzyme in arginine synthesis and the urea cycle, which are highly conserved from bacteria to eukaryotes. The gene encoding Streptococcus mutans ASL (smASL) was amplified and cloned into expression vector pET28a. The recombinant smASL protein was expressed in a soluble form in Escherichia coli strain BL21 (DE3) and purified to homogeneity by two-step column chromatography. Crystals suitable for X-ray analysis were obtained and X-ray diffraction data were collected to a resolution of 2.5 Å. The crystals belonged to space group R3, with unit-cell parameters a = b = 254.5, c = 78.3 Å.

AB - Argininosuccinate lyase (ASL) is an important enzyme in arginine synthesis and the urea cycle, which are highly conserved from bacteria to eukaryotes. The gene encoding Streptococcus mutans ASL (smASL) was amplified and cloned into expression vector pET28a. The recombinant smASL protein was expressed in a soluble form in Escherichia coli strain BL21 (DE3) and purified to homogeneity by two-step column chromatography. Crystals suitable for X-ray analysis were obtained and X-ray diffraction data were collected to a resolution of 2.5 Å. The crystals belonged to space group R3, with unit-cell parameters a = b = 254.5, c = 78.3 Å.

KW - argininosuccinate lyase

KW - Streptococcus mutans

UR - http://www.scopus.com/inward/record.url?scp=79958101763&partnerID=8YFLogxK

U2 - 10.1107/S1744309111011377

DO - 10.1107/S1744309111011377

M3 - Journal article

C2 - 21636911

AN - SCOPUS:79958101763

VL - 67

SP - 682

EP - 684

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - 6

ER -

ID: 234874408