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Three-dimensional structure of beta-galactosidase from E. coli
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title
Three-dimensional structure of beta-galactosidase from E. coli
(English)
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main subject
Escherichia coli
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author name string
R H Jacobson
series ordinal
1
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X J Zhang
series ordinal
2
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R F DuBose
series ordinal
3
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B W Matthews
series ordinal
4
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language of work or name
English
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publication date
30 June 1994
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published in
Nature
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volume
369
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page(s)
761-6
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issue
6483
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cites work
Genetic regulatory mechanisms in the synthesis of proteins
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Sequence of the lacZ gene of Escherichia coli
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Crossref
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Crystallization of beta-galactosidase from Escherichia coli
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Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
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Relation between structure and function of alpha/beta-proteins
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An immunological study of complementary fragments of beta-galactosidase
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Multiple replacements establish the importance of tyrosine-503 in beta-galactosidase (Escherichia coli).
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Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the β-galactosidase structural gene of Escherichia coli
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Molecular basis of beta-galactosidase alpha-complementation
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beta-Galactosidase alpha-complementation. A model of protein-protein interaction
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Unbiased three-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
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Nucleotide sequence of Klebsiella pneumoniae lac genes
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Analysis of the lacZ sequences from two Streptococcus thermophilus strains: comparison with the Escherichia coli and Lactobacillus bulgaricus beta-galactosidase sequences
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Expression and nucleotide sequence of the Clostridium acetobutylicum beta-galactosidase gene cloned in Escherichia coli
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3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin
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Structure of a human common cold virus and functional relationship to other picornaviruses
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Identifiers
DOI
10.1038/369761A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2675181
Dimensions Publication ID
1002787672
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OpenCitations bibliographic resource ID
2675181
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2675181
PubMed ID
8008071
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2675181
Springer Nature article ID
10.1038/369761a0
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