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 journalArticlepeer-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 languageEnglish
Pages (from-to)1482-1483
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number9
DOIs
Publication statusPublished - Sep 2002
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

Fingerprint

Dive into the research topics of 'Crystallization and preliminary crystallographic analysis of a D-aminoacylase from Alcaligenes faecalis DA1'. Together they form a unique fingerprint.

Cite this