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

Ionic strength reducers: an efficient approach to protein purification and crystallization. Application to two Rop variants.

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

Papanikolau Yannis, Kotsifaki Dina, Fadouloglou Vasiliki E, Gazi Anastasia D, Glykos Nicholas M, Cesareni Giovanni, Kokkinidis Michael

Abstract excerpt

Detailed knowledge of the influence of various parameters on macromolecular solubility is essential for crystallization. The concept of so-called 'ionic strength reducers' provides insight into the changes in solubility induced by organic solvents and hydrophilic polymers in aqueous electrolytic...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Bacterial Proteins
Share to Crystallization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Mutation

Share to Osmolar Concentration

Share to RNA-Binding Proteins

Source

Identifiers

PMID: 15213408
DOI: 10.1107/S0907444904008546

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-15213408-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ionic strength reducers: an efficient approach to protein purification and crystallization. Application to two Rop variants.PMID 15213408Read ↗

Correlation between protein stability and crystal properties of designed ROP variants.Semantic proximity Read ↗

Direct identification of a siderophore import protein using synthetic petrobactin ligands.Semantic proximity Read ↗

Detection and prevention of protein aggregation before, during, and after purification.Semantic proximity Read ↗

Crystallization of type I chloramphenicol acetyltransferase: an approach based on the concept of ionic strength reducers.Semantic proximity Read ↗

Guidelines for the successful generation of protein-ligand complex crystals.Semantic proximity Read ↗

SAS: Split Antibiotic Selection for identifying chaperones that improve protein solubilitySemantic proximity Read ↗

Recombinant production of the human aquaporins in the yeast<i>Pichia pastoris</i>(Invited Review)Semantic proximity Read ↗

Efficient protein production inspired by how spiders make silk.Semantic proximity Read ↗

Crystallization and diffraction to ultrahigh resolution (0.8 A) of a designed variant of the Rop protein.Semantic proximity Read ↗

The bigger picture: global analysis of solubilization performance of classical detergents versus new synthetic polymers utilizing shotgun proteomicsSemantic proximity Read ↗

Structure-based substitutions for increased solubility of a designed protein.Semantic proximity Read ↗

Amino Acids as Building Blocks for Carbonic Anhydrase InhibitorsSemantic proximity Read ↗

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