Open AccessPreliminary crystallographic analysis of the Escherichia coli YeaZ protein using the anomalous signal of a gadolinium derivative
Author(s) -
Kahn Richard,
Jeudy Sandra,
Stelter Meike,
Coutard Bruno,
Abergel Chantal
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105025856
Subject(s) - gadolinium , orthorhombic crystal system , escherichia coli , crystallography , chemistry , resolution (logic) , derivative (finance) , crystal (programming language) , crystal structure , gene , biochemistry , organic chemistry , artificial intelligence , computer science , financial economics , economics , programming language
The Escherichia coli yeaZ gene encodes a 231‐residue protein ( M r = 25 180) that belongs to a family of proteins that are conserved in various bacterial genomes. This protein of unknown function is predicted to be a hypothetical protease. The YeaZ protein was overexpressed in E. coli and crystallized at 298 K by the hanging‐drop vapour‐diffusion method. A MAD data set was collected using a gadolinium‐derivative crystal that had been soaked with 0.1 M Gd‐DOTMA. The data set contained data collected to a resolution of 2.7 Å at two wavelengths at the L III absorption edge of gadolinium, while remote data were collected to a resolution of 2.28 Å. The crystal belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 76.3, b = 97.6, c = 141.9 Å. Phasing using the MAD method confirmed there to be four monomers in the asymmetric unit related by two twofold axes as identified by the self‐rotation function search.