𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Crystallization and preliminary X-ray analysis of L-2-haloacid dehalogenase from xanthobacter autotrophicus GJ10

✍ Scribed by Ivo S. Ridder; Henriëtte J. Rozeboom; Bauke W. Dijkstra; Jaap Kingma; Dick B. Janssen

Book ID
105356361
Publisher
Cold Spring Harbor Laboratory Press
Year
1995
Tongue
English
Weight
225 KB
Volume
4
Category
Article
ISSN
0961-8368

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

Haloacid dehalogenases are enzymes that cleave carbon‐chlorine or carbon‐bromine bonds of 2‐haloalkanoates. X‐ray‐quality crystals of L‐2‐haloacid dehalogenase from the 1, 2‐dichloroethane‐degrading bacterium Xanthobacter autotrophicus GJ10 have been grown at room temperature from 20% PEG 8000, 200 mM sodium formate at pH 6.8‐7.0, using macroseeding techniques. The crystals, which diffract in the X‐ray beam up to 2.0 Å resolution, belong to the spacegroup C222~1~. Cell parameters are a = 58.8 Å, b = 93.1 Å, c = 84.2 Å. A native data set to 2.3 Å has been collected, with a completeness of 97% and an R~sym~ of 6.0%.

📜 SIMILAR VOLUMES

Crystallization and preliminary X-ray cr
Crystallization and preliminary X-ray crystallographic analysis of phosphoribulokinase from Rhodobacter sphaeroides
✍ David L. Roberts; Jennifer A. Runquist; Henry M. Miziorko; Jung-Ja P. Kim 📂 Article 📅 1995 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 914 KB

## Abstract A recombinant form of __Rhodobacter sphaeroides__ phosphoribulokinase (PRK), expressed in __Escherichia coli__ and isolated by affinity chromatography, was crystallized by the sitting drop vapor diffusion technique using NH~4~H~2~PO~4~ (pH 5.6) as the precipitating agent. PRK crystalliz