Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1

Cheng Sheng Hsu; Shen Jia Chen; Ying Chieh Tsai; Ting Wan Lin; Shwu Huey Liaw; Andrew H.J. Wang

doi:10.1107/S0907444902011046

Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1

Cheng Sheng Hsu, Shen Jia Chen, Ying Chieh Tsai, Ting Wan Lin, Shwu Huey Liaw, Andrew H.J. Wang

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

3 Citations (Scopus)

Abstract

D-Aminoacylases catalyze the hydrolysis of N-acyl-D-amino acids into D-amino acids with the aid of zinc ions. The first D-aminoacylase crystal from Alcaligenes faecalis has been obtained in hanging drops at pH 5.6 by the vapour-diffusion method using 30% polyethylene glycol 4000 as precipitant. It belongs to space group P2₁2₁2₁, with unit-cell parameters a = 60.2, b = 76.6, c = 135.3 Å. Reflections to 1.2 Å resolution are observable. An initial atomic model with 472 residues has been built based on SeMet SAD data at 1.8 Å resolution. Unexpectedly, the structure revealed a novel metal centre in the amidohydrolase superfamily.

Original language	English
Pages (from-to)	1482-1483
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	58
Issue number	9
DOIs	https://doi.org/10.1107/S0907444902011046
Publication status	Published - Sept 2002
Externally published	Yes

ASJC Scopus subject areas

Structural Biology

Access to Document

10.1107/S0907444902011046

Cite this

@article{d420f530a6e04c75be82971930060df5,

title = "Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1",

abstract = "D-Aminoacylases catalyze the hydrolysis of N-acyl-D-amino acids into D-amino acids with the aid of zinc ions. The first D-aminoacylase crystal from Alcaligenes faecalis has been obtained in hanging drops at pH 5.6 by the vapour-diffusion method using 30% polyethylene glycol 4000 as precipitant. It belongs to space group P212121, with unit-cell parameters a = 60.2, b = 76.6, c = 135.3 {\AA}. Reflections to 1.2 {\AA} resolution are observable. An initial atomic model with 472 residues has been built based on SeMet SAD data at 1.8 {\AA} resolution. Unexpectedly, the structure revealed a novel metal centre in the amidohydrolase superfamily.",

author = "Hsu, {Cheng Sheng} and Chen, {Shen Jia} and Tsai, {Ying Chieh} and Lin, {Ting Wan} and Liaw, {Shwu Huey} and Wang, {Andrew H.J.}",

year = "2002",

month = sep,

doi = "10.1107/S0907444902011046",

language = "English",

volume = "58",

pages = "1482--1483",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "John Wiley and Sons Inc.",

number = "9",

}

TY - JOUR

T1 - Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1

AU - Hsu, Cheng Sheng

AU - Chen, Shen Jia

AU - Tsai, Ying Chieh

AU - Lin, Ting Wan

AU - Liaw, Shwu Huey

AU - Wang, Andrew H.J.

PY - 2002/9

Y1 - 2002/9

N2 - D-Aminoacylases catalyze the hydrolysis of N-acyl-D-amino acids into D-amino acids with the aid of zinc ions. The first D-aminoacylase crystal from Alcaligenes faecalis has been obtained in hanging drops at pH 5.6 by the vapour-diffusion method using 30% polyethylene glycol 4000 as precipitant. It belongs to space group P212121, with unit-cell parameters a = 60.2, b = 76.6, c = 135.3 Å. Reflections to 1.2 Å resolution are observable. An initial atomic model with 472 residues has been built based on SeMet SAD data at 1.8 Å resolution. Unexpectedly, the structure revealed a novel metal centre in the amidohydrolase superfamily.

AB - D-Aminoacylases catalyze the hydrolysis of N-acyl-D-amino acids into D-amino acids with the aid of zinc ions. The first D-aminoacylase crystal from Alcaligenes faecalis has been obtained in hanging drops at pH 5.6 by the vapour-diffusion method using 30% polyethylene glycol 4000 as precipitant. It belongs to space group P212121, with unit-cell parameters a = 60.2, b = 76.6, c = 135.3 Å. Reflections to 1.2 Å resolution are observable. An initial atomic model with 472 residues has been built based on SeMet SAD data at 1.8 Å resolution. Unexpectedly, the structure revealed a novel metal centre in the amidohydrolase superfamily.

UR - http://www.scopus.com/inward/record.url?scp=0036712144&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036712144&partnerID=8YFLogxK

U2 - 10.1107/S0907444902011046

DO - 10.1107/S0907444902011046

M3 - Article

C2 - 12198309

AN - SCOPUS:0036712144

SN - 0907-4449

VL - 58

SP - 1482

EP - 1483

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 9

ER -

Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this