Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Errors in three dimensions.

J Janin1

  • 1Laboratoire de Biologie Physicochimique, UA 1131, Université Paris-Sud, Orsay, France.

Biochimie
|October 1, 1990
PubMed
Summary
This summary is machine-generated.

Protein structure precision is crucial. Crystallography and NMR spectroscopy aim for high accuracy, with errors correctable during refinement, but data deposition remains vital.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A new protein-protein docking scoring function based on interface residue properties.

Bioinformatics (Oxford, England)·2007
Same author

Encapsulation of mono- and oligo-nucleotides into aqueous-core nanocapsules in presence of various water-soluble polymers.

International journal of pharmaceutics·2006
Same author

Encapsulation of antiviral nucleotide analogues azidothymidine-triphosphate and cidofovir in poly(iso-butylcyanoacrylate) nanocapsules.

International journal of pharmaceutics·2006
Same author

Adenosine phosphonoacetic acid is slowly metabolized by NDP kinase.

Medicinal chemistry (Shariqah (United Arab Emirates))·2006
Same author

Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymes.

Biochimie·2005
Same author

Three-dimensional structure of nucleoside diphosphate kinase.

Journal of bioenergetics and biomembranes·2002
Same journal

Differential cardiac microRNA expression in anoxic Trachemys scripta elegans turtles.

Biochimie·2026
Same journal

Renal failure-driven luminal ammonia production impairs gut barrier function in CKD.

Biochimie·2026
Same journal

Conditional Knockout of Indoleamine 2, 3-Dioxygenase-1 in Osteoprogenitor Cells in Mice Results in Sex-dependent Differences in Bone Mass.

Biochimie·2026
Same journal

Sedentariness disrupts, while exercise restores, thermogenic and metabolic plasticity in inguinal adipose tissue of mice.

Biochimie·2026
Same journal

Chrononutrition as a modulator of retinal metabolic resilience: A translational framework linking circadian biology to ocular disease.

Biochimie·2026
Same journal

Heterologous expression, purification, and biophysical characterisation of the cobalt-dependent nitrile hydratase from Rhodococcus rhodochrous ATCC BAA-870.

Biochimie·2026
See all related articles

Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Concerns exist regarding the accuracy of published protein structures, particularly X-ray crystallography data.
  • The precision of three-dimensional (3D) protein structures is a critical consideration for researchers.

Purpose of the Study:

  • To assess and discuss the achievable precision of protein structures determined by X-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy.
  • To emphasize the importance of data deposition in protein structure databases.

Main Methods:

  • Analysis of error correction during crystallographic refinement.
  • Evaluation of precision based on homologous protein structures.
  • Assessment of NMR structure precision using Nuclear Overhauser Effect (NOE) constraints.

Related Experiment Videos

Main Results:

  • Crystallographic refinement can correct errors, aiming for 0.15–0.25 Å precision at high resolution.
  • Independent estimates suggest common precision better than 0.5 Å for Cα and main chain atoms in crystal structures.
  • NMR structures can achieve better than 2 Å precision with sufficient NOE constraints.

Conclusions:

  • High precision is achievable in protein structure determination through both crystallography and NMR.
  • Despite potential errors, depositing atomic coordinates in databases is essential for scientific progress.