Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.

Acta crystallographica. Section D, Biological crystallography - 1 Nov 2004

Kogan Anna, Gdalevsky Garik Y, Cohen-Luria Rivka, Parola Abraham H, Goldgur Yehuda

Abstract excerpt

Tryptophanase from Escherichia coli is a pyridoxal phosphate-dependent homotetrametic enzyme with a subunit weight of 52 kDa. It has been crystallized in the apo form by the hanging-drop vapour-diffusion method using polyethylene glycol 400 as a precipitant and magnesium chloride as an additive. The crystals belong to the orthorhombic space group F222, with unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apoenzymes
Share to Crystallization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Escherichia coli

Share to Mutation

Share to Tryptophan

Share to Tyrosine

Source

Identifiers

PMID: 15502331
DOI: 10.1107/S0907444904022425

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.PMID 15502331Read ↗

Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli.Semantic proximity Read ↗

Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli.Semantic proximity Read ↗

The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.Semantic proximity Read ↗

A structural view of the dissociation of Escherichia coli tryptophanase.Semantic proximity Read ↗

A Molecular Dynamics Simulation Study of the Effects of βGln114 Mutation on the Dynamic Behavior of the Catalytic Site of the Tryptophan Synthase.Semantic proximity Read ↗

Crystallization and preliminary X-ray analysis of W120K mutant of streptavidin.Semantic proximity Read ↗

Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a beta-ketoacyl carrier protein reductase homologue.Semantic proximity Read ↗

Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon.Semantic proximity Read ↗

Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.Semantic proximity Read ↗

Recombinant protein production driven by the tryptophan promoter is tightly controlled in ICONE 200, a new genetically engineered E. coli mutant.Semantic proximity Read ↗

Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.Semantic proximity Read ↗

Cold inactivation and dissociation into dimers of Escherichia coli tryptophanase and its W330F mutant form.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.