Crystal structure and mechanism of the lytic transglycosylase MltA from Escherichia coli

Karin van Straaten

Crystal structure and mechanism of the lytic transglycosylase MltA from Escherichia coli

Karin van Straaten

X-ray Crystallography

Research output: Thesis › Thesis fully internal (DIV)

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Abstract

This thesis describes the determination and analysis of the 3D-structure of the lytic transglycosylase MltA from Escherichia coli by X-ray crystallography. This work aims to further increase our knowledge of the molecular details of the cleaving mechanism and the typical 1,6- anhydromuropeptide production by the lytic transglycosylases from Escherichia Coli Zie: Summary

Original language	English
Qualification	Doctor of Philosophy
Awarding Institution	University of Groningen
Supervisors/Advisors	Dijkstra, B.W., Supervisor Thunnissen, Andy, Supervisor
Award date	8-May-2006
Place of Publication	Groningen
Publisher	s.n.
Publication status	Published - 2006

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abstract = "This thesis describes the determination and analysis of the 3D-structure of the lytic transglycosylase MltA from Escherichia coli by X-ray crystallography. This work aims to further increase our knowledge of the molecular details of the cleaving mechanism and the typical 1,6- anhydromuropeptide production by the lytic transglycosylases from Escherichia Coli Zie: Summary",

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N2 - This thesis describes the determination and analysis of the 3D-structure of the lytic transglycosylase MltA from Escherichia coli by X-ray crystallography. This work aims to further increase our knowledge of the molecular details of the cleaving mechanism and the typical 1,6- anhydromuropeptide production by the lytic transglycosylases from Escherichia Coli Zie: Summary

AB - This thesis describes the determination and analysis of the 3D-structure of the lytic transglycosylase MltA from Escherichia coli by X-ray crystallography. This work aims to further increase our knowledge of the molecular details of the cleaving mechanism and the typical 1,6- anhydromuropeptide production by the lytic transglycosylases from Escherichia Coli Zie: Summary

M3 - Thesis fully internal (DIV)

PB - s.n.

CY - Groningen

ER -