Evidence map›Paper›PMID 22339624›Full record

ArticleJournal of the American Chemical Society2012

Growth rates of protein crystals.

Jeremy D Schmit, Ken Dill

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. Article
  2. A multiscaleJournal of applied crystallography · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The "speed limit" for macromolecular crystal growth.Protein science : a publication of the Protein Society · 2018
    Article
  9. Theory of Sequence Effects in Amyloid Aggregation.The journal of physical chemistry. B · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. A strategy for selecting the pH of protein solutions to enhance crystallization.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Jeremy D SchmitDepartment of Physics, Kansas State University, Manhattan, Kansas 66506, USA. Schmit@phys.ksu.edu
Ken Dill

Funding

COMBINATORIAL STATISTICAL MECHANICS OF PROTEIN FOLDINGR01GM034993 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DILL, KEN A · 1985 to 2009
$2.7M
NIGMS NIH HHS GM34993NIGMS NIH HHS R01 GM034993
6 · The paper itself

Abstract

Protein crystallization is important for structural biology. The rate at which a protein crystallizes is often the bottleneck in determining the protein's structure. Here, we give a physical model for the growth rates of protein crystals. Most materials crystallize faster under stronger growth conditions; however, protein crystallization slows down under the strongest conditions. Proteins require a crystallization slot of 'just right' conditions. Our model provides an explanation. Unlike simpler materials, proteins are orientationally asymmetrical. Under strong conditions, protein molecules attempt to crystallize too quickly, in wrong orientations, blocking surface sites for more productive crystal growth. The model explains the observation that increasing the net charge on a protein increases the crystal growth rate. The model predictions are in good agreement with experiments on the growth rates of tetragonal lysozyme crystals as a function of pH, salt concentration, temperature, and protein concentration.

Indexed as

CrystallizationModels, MolecularMuramidaseProtein ConformationThermodynamicsMuramidase

Identifiers

PMID22339624
PMCPMC3311159

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.