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Initial evaluations of the reproducibility of vapor-diffusion crystallization

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/s00018-003-3260-zopenalex-snapshot
Which strategy for a protein crystallization project?
inferredcites →https://doi.org/10.1016/j.ymeth.2004.03.031openalex-snapshot
Predictive models for protein crystallization
inferredcites →https://doi.org/10.1016/s0021-9258(19)86452-9openalex-snapshot
Protein crystallization using incomplete factorial experiments.
inferredcites →https://doi.org/10.1016/s0022-0248(01)01154-xopenalex-snapshot
Efficiency analysis of sampling protocols used in protein crystallization screening
inferredcites →https://doi.org/10.1021/ja9930869openalex-snapshot
Are Nucleation Kinetics of Protein Crystals Similar to Those of Liquid Droplets?
inferredcites →https://doi.org/10.1074/jbc.273.35.22420openalex-snapshot
Motion of the DNA-binding Domain with Respect to the Core of the Diphtheria Toxin Repressor (DtxR) Revealed in the Crystal Structures of Apo- and Holo-DtxR
inferredcites →https://doi.org/10.1107/s0021889804028055openalex-snapshot
Reduction in diffuso-convective disturbances in nanovolume protein crystallization experiments
inferredcites →https://doi.org/10.1107/s0021889806029979openalex-snapshot
XtalBase– a comprehensive data management system for macromolecular crystallography
inferredcites →https://doi.org/10.1107/s0021889891004430openalex-snapshot
Sparse matrix sampling: a screening method for crystallization of proteins

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.3582695openalex-extracted
Predicting the Effect of Chemical Factors on the pH of Crystallisation Trials
inferred← citeshttps://doi.org/10.1002/crat.201100178openalex-snapshot
The effect of diluting crystallization droplets on protein crystallization in vapor diffusion method
inferred← citeshttps://doi.org/10.1002/prot.26844openalex-snapshot
Using AlphaFold and Symmetrical Docking to Predict Protein–Protein Interactions for Exploring Potential Crystallization Conditions
inferred← citeshttps://doi.org/10.1007/978-1-4939-2230-7_8openalex-snapshot
Crystallization: Digging into the Past to Learn Lessons for the Future
inferred← citeshttps://doi.org/10.1007/s11433-012-4640-xopenalex-snapshot
Effect of protein molecular weight on the mass transfer in protein mixing
inferred← citeshttps://doi.org/10.1007/s13738-020-02058-yopenalex-snapshot
Macromolecular crystallization: basics and advanced methodologies
inferred← citeshttps://doi.org/10.1016/j.ab.2022.114594openalex-snapshot
The reproducible normality of the crystallographic B-factor
inferred← citeshttps://doi.org/10.1016/j.apsusc.2022.155029openalex-snapshot
Laser ablation combined with Nanoimprint Lithography technology as new surface engineering approach to produce novel polymer-based heteronucleants for recalcitrant protein crystallization
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.08.161openalex-snapshot
A hetero-micro-seeding strategy for readily crystallizing closely related protein variants
inferred← citeshttps://doi.org/10.1016/j.bpc.2023.107027openalex-snapshot
Linking B-factor and temperature-induced conformational transition
inferred← citeshttps://doi.org/10.1016/j.cherd.2021.06.012openalex-snapshot
The critical role of agitation in moving from preliminary screening results to reproducible batch protein crystallisation
inferred← citeshttps://doi.org/10.1016/j.isci.2020.101219openalex-snapshot
Predicting the Effect of Chemical Factors on the pH of Crystallization Trials
inferred← citeshttps://doi.org/10.1016/j.snb.2012.08.048openalex-snapshot
Fabrication of X-ray compatible microfluidic platforms for protein crystallization
inferred← citeshttps://doi.org/10.1016/j.xphs.2018.04.018openalex-snapshot
Application of Empirical Phase Diagrams for Multidimensional Data Visualization of High-Throughput Microbatch Crystallization Experiments
inferred← citeshttps://doi.org/10.1016/j.ymeth.2011.04.004openalex-snapshot
One plate, two plates, a thousand plates. How crystallisation changes with large numbers of samples
inferred← citeshttps://doi.org/10.1021/acsomega.5c13533openalex-snapshot
Pinpointing Protein Crystal Structures over a Broad Temperature Range Using Hydrophobic Protection
inferred← citeshttps://doi.org/10.1021/cg1013945openalex-snapshot
What’s in a Drop? Correlating Observations and Outcomes to Guide Macromolecular Crystallization Experiments
inferred← citeshttps://doi.org/10.1021/cg3011212openalex-snapshot
Microfluidic Approach to Cocrystal Screening of Pharmaceutical Parent Compounds
inferred← citeshttps://doi.org/10.1021/cg4014569openalex-snapshot
Using Time Courses To Enrich the Information Obtained from Images of Crystallization Trials
inferred← citeshttps://doi.org/10.1038/srep07797openalex-snapshot
An ignored variable: solution preparation temperature in protein crystallization
inferred← citeshttps://doi.org/10.1039/c7ce00664kopenalex-snapshot
Combined cross-diffusion microbatch method and seeding technique to enhance protein crystallization based on a common dispersing agent
inferred← citeshttps://doi.org/10.1039/d1ce00026hopenalex-snapshot
Enhancing the crystallisation of insulin using amino acids as soft-templates to control nucleation
inferred← citeshttps://doi.org/10.1039/d2lc01194hopenalex-snapshot
Polymer-based microfluidic device for on-chip counter-diffusive crystallization and in situ X-ray crystallography at room temperature
inferred← citeshttps://doi.org/10.1093/bioinformatics/btv011openalex-snapshot
Using isoelectric point to determine the pH for initial protein crystallization trials
inferred← citeshttps://doi.org/10.1101/2025.07.08.662548openalex-snapshot
Pinpointing protein structures over broad temperature range using hydrophobic protection
inferred← citeshttps://doi.org/10.1107/s0021889813008030openalex-snapshot
The current approach to initial crystallization screening of proteins is under-sampled
inferred← citeshttps://doi.org/10.1107/s0907444913016296openalex-snapshot
A quality comparison of protein crystals grown under containerless conditions generated by diamagnetic levitation, silicone oil and agarose gel
inferred← citeshttps://doi.org/10.1107/s1600576717007312openalex-snapshot
The nucleation of protein crystals as a race against time with on- and off-pathways
inferred← citeshttps://doi.org/10.1107/s1600576725000457openalex-snapshot
A generic cross-seeding approach to protein crystallization
inferred← citeshttps://doi.org/10.1107/s1744309108029667openalex-snapshot
Phoenito experiments: combining the strengths of commercial crystallization automation
inferred← citeshttps://doi.org/10.1107/s2053230x14011601openalex-snapshot
Automation in biological crystallization
inferred← citeshttps://doi.org/10.1107/s2053230x1401262xopenalex-snapshot
Crystallization screening: the influence of history on current practice
inferred← citeshttps://doi.org/10.1107/s2053230x14019244openalex-snapshot
Enhancing ubiquitin crystallization through surface-entropy reduction
inferred← citeshttps://doi.org/10.1107/s2053230x15008626openalex-snapshot
Trace fluorescent labeling for protein crystallization
inferred← citeshttps://doi.org/10.1107/s2053230x16000030openalex-snapshot
The role of mass transport in protein crystallization
inferred← citeshttps://doi.org/10.1107/s2053230x19000141openalex-snapshot
BLAST ing away preconceptions in crystallization trials
inferred← citeshttps://doi.org/10.1107/s2059798315024687openalex-snapshot
Lessons from ten years of crystallization experiments at the SGC
inferred← citeshttps://doi.org/10.1177/2211068215598938openalex-snapshot
Developments in the Implementation of Acoustic Droplet Ejection for Protein Crystallography
inferred← citeshttps://doi.org/10.3791/55790openalex-snapshot
Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology
inferred← citeshttps://doi.org/10.3791/55790-vopenalex-snapshot
Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology
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