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

Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant.

Acta crystallographica. Section D, Biological crystallography - 1 Jun 2003

Miele Adriana E, Federici Luca, Sciara Giuliano, Draghi Federica, Brunori Maurizio, Vallone Beatrice

Abstract excerpt

Crystals of the Met derivative of the sperm whale myoglobin triple mutant Mb-YQR [L(B10)Y, H(E7)Q and T(E10)R] were grown under microgravity conditions and on earth by vapour diffusion. A comparison of crystal quality after complete data collection and processing shows how microgravity-grown crystals diffract to better resolution and lead to considerably improved statistics for X-ray diffraction data compared...

Read the complete abstract on PubMed

Topics

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

Share to Crystallization
Share to Electrons

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

Share to Myoglobin

Share to Oxidation-Reduction

Share to Space Flight

Share to Weightlessness

Share to X-Ray Diffraction

Source

Identifiers

PMID: 12777759
DOI: 10.1107/s0907444903005924

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

Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant.PMID 12777759Read ↗

Crystal structure of Asian elephant (Elephas maximus) cyano-metmyoglobin at 1.78-A resolution. Phe29(B10) accounts for its unusual ligand binding properties.Semantic proximity Read ↗

Structural dynamics of myoglobin.Semantic proximity Read ↗

Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10).Semantic proximity Read ↗

Exploring Compactness and Dynamics of Apomyoglobin.Semantic proximity Read ↗

Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.Semantic proximity Read ↗

Factors correlating with significant differences between X-ray structures of myoglobin.Semantic proximity Read ↗

Crystallizing the Parkinson’s Disease Protein LRRK2 Under Microgravity ConditionsSemantic proximity Read ↗

The heme iron coordination complex in His64(E7)Tyr recombinant sperm whale myoglobin.Semantic proximity Read ↗

The evolutionary footprint of histidine in hemoglobin and myoglobin: an implication towards their function.Semantic proximity Read ↗

Fast purification of the Apo form and of a non-binding heme mutant of recombinant sperm whale myoglobin.Semantic proximity Read ↗

Pattern of cavities in globins: the case of human hemoglobin.Semantic proximity Read ↗

Towards a "Golden Standard" for computing globin stability: Stability and structure sensitivity of myoglobin mutants.Semantic proximity Read ↗

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