Literature summary for 6.3.2.8 extracted from

Deva, T.; Baker, E.N.; Squire, C.J.; Smith, C.A.
Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC) (2006), Acta Crystallogr. Sect. D, 62, 1466-1474.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase determined to 2.6 A resolution. The structure is solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212. Crystals of both native and SeMet-substituted EcMurC belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 73.9 A, b = 93.6 A, c = 176.8 A. The SeMet crystals give the best quality diffraction data	Escherichia coli

Crystallization (Comment)

Organism

crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase determined to 2.6 A resolution. The structure is solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212. Crystals of both native and SeMet-substituted EcMurC belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 73.9 A, b = 93.6 A, c = 176.8 A. The SeMet crystals give the best quality diffraction data

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P17952	-	-

Synonyms

Synonyms	Comment	Organism
MurC	-	Escherichia coli
UDP-N-acetylmuramoyl:L-alanine ligase	-	Escherichia coli

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Release 2023.1 (January 2023)