(Q54706014)

3 June 2018

title

Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP. (English)

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3 June 2018

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Brunie S

1

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3 June 2018

Zelwer C

series ordinal

2

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3 June 2018

Risler JL

series ordinal

3

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3 June 2018

language of work or name

English

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publication date

1 November 1990

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3 June 2018

Journal of Molecular Biology

published in

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3 June 2018

volume

216

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3 June 2018

issue

2

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3 June 2018

page(s)

411-424

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3 June 2018

Recognition of a DNA operator by the repressor of phage 434: a view at high resolution

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Conserved cysteine and histidine residues in the structures of the tyrosyl and methionyl-tRNA synthetases

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Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold

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Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases

7 January 2021

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Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 A resolution

7 January 2021

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Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

The distribution of phase angles for structures containing heavy atoms. II. A modification of the normal heavy-atom method for non-centrosymmetrical structures

1 reference

19 October 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0365110X59002316

Identifiers

DOI

10.1016/S0022-2836(05)80331-6

1 reference

3 June 2018

1 reference

3 June 2018