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Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli.
Acta Crystallogr D Biol Crystallogr. 2004 Apr; 60(Pt 4):758-60.AC

Abstract

The lytic transglycosylase MltA from Escherichia coli with its membrane anchor and signal sequence deleted has been purified to homogeneity by means of cation-exchange chromatography. The enzyme was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 103.70, c = 109.84 A and one molecule per asymmetric unit. Crystals diffract to 2.2 A resolution on a synchrotron-radiation source.

Authors+Show Affiliations

Van Straaten KE
Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Dijkstra BW
No affiliation info available
Thunnissen AM
No affiliation info available

MeSH

Cloning, MolecularCrystallizationCrystallography, X-RayEscherichia coli ProteinsGlycosyltransferasesMutationSolubility

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15039577

Citation

Van Straaten, Karin E., et al. "Purification, Crystallization and Preliminary X-ray Analysis of the Lytic Transglycosylase MltA From Escherichia Coli." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 4, 2004, pp. 758-60.
Van Straaten KE, Dijkstra BW, Thunnissen AM. Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):758-60.
Van Straaten, K. E., Dijkstra, B. W., & Thunnissen, A. M. (2004). Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 4), 758-60.
Van Straaten KE, Dijkstra BW, Thunnissen AM. Purification, Crystallization and Preliminary X-ray Analysis of the Lytic Transglycosylase MltA From Escherichia Coli. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):758-60. PubMed PMID: 15039577.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli. AU - Van Straaten,Karin E, AU - Dijkstra,Bauke W, AU - Thunnissen,Andy Mark W H, Y1 - 2004/03/23/ PY - 2003/12/18/received PY - 2004/02/02/accepted PY - 2004/3/25/pubmed PY - 2004/12/16/medline PY - 2004/3/25/entrez SP - 758 EP - 60 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 4 N2 - The lytic transglycosylase MltA from Escherichia coli with its membrane anchor and signal sequence deleted has been purified to homogeneity by means of cation-exchange chromatography. The enzyme was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 103.70, c = 109.84 A and one molecule per asymmetric unit. Crystals diffract to 2.2 A resolution on a synchrotron-radiation source. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15039577/Purification_crystallization_and_preliminary_X_ray_analysis_of_the_lytic_transglycosylase_MltA_from_Escherichia_coli_ DB - PRIME DP - Unbound Medicine ER -