http://orcid.org/0000-0003-0608-7875
References
- Grey JL, Thompson DH. Challenges and opportunities for new protein crystallization strategies in structure-based drug design. Expert Opin Drug Discov. 2010;5:1039–1045.
- Heck GS, Pintro VO, Pereira RR, et al. Supervised machine learning methods applied to predict ligand- binding affinity. Curr Med Chem. 2017;24:2459–2470.
- Burley SK, Berman HM, Christie C, et al. Rcsb protein data bank: sustaining a living digital data resource that enables breakthroughs in scientific research and biomedical education. Protein Sci. 2018;27:316–330.
- Burley SK, Berman HM, Kleywegt GJ, et al. Protein data bank (PDB): the single global macromolecular structure archive. Methods Mol Biol. 2017;1607:627–641.
- de Azevedo WF Jr., Canduri F, Basso LA, et al. Determining the structural basis for specificity of ligands using crystallographic screening. Cell Biochem Biophys. 2006;44:405–411.
- Canduri F, de Azevedo WF. Protein crystallography in drug discovery. Curr Drug Targets. 2008;9:1048–1053.
- Luft JR, Snell EH, Detitta GT. Lessons from high-throughput protein crystallization screening: 10 years of practical experience. Expert Opin Drug Discov. 2011;6:465–480.
- Elsliger MA, Deacon AM, Godzik A, et al. The jcsg high-throughput structural biology pipeline. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010;66:1137–1142.
- Skarina T, Xu X, Evdokimova E, et al. High-throughput crystallization screening. Methods Mol Biol. 2014;1140:159–168.
- Lekamge B, Sowmya A, Newman J. Prediction of protein x-ray crystallisation trial image time-courses. In: Marsico DM, Baja GS, Fred A, editors. Proceedings of the 6th International Conference on Pattern Recognition Applications and Methods. Setúbal: SciTePress; 2017. p. 663–668.
- Dong A, Xu X, Edwards AM, et al. In situ proteolysis for protein crystallization and structure determination. Nat Methods. 2007;4:1019–1021.
- Derewenda ZS, Vekilov PG. Entropy and surface engineering in protein crystallization. Acta Crystallogr D Biol Crystallogr. 2006;62:116–124.
- McPherson A, Cudney B. Searching for silver bullets: an alternative strategy for crystallizing macromolecules. J Struct Biol. 2006;156:387–406.
- Chruszcz M, Zimmerman MD, Wang S, et al. Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from pseudomonas aeruginosa pao1. Cryst Growth Des. 2008;8:4054–4061.
- Milic D, Veprintsev DB. Large-scale production and protein engineering of g protein-coupled receptors for structural studies. Front Pharmacol. 2015;6:66.
- Russo Krauss I, Merlino A, Vergara A, et al. An overview of biological macromolecule crystallization. Int J Mol Sci. 2013;14(6):11643–11691.
- Moreno A. Advanced methods of protein crystallization. Methods Mol Biol. 2017;1607:51–76.
- Schieferstein JM, Pawate AS, Sun C, et al. X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization. Biomicrofluidics. 2017;11:024118.
- Jancarik J, Kim S-H. Sparse matrix sampling: a screening method for crystallization of proteins. J Appl Cryst. 1991;24:409–411.
- Ng JT, Dekker C, Reardon P, et al. Lessons from ten years of crystallization experiments at the SCG. Acta Crystallogr D Struct Biol. 2016;72:224–235.
- Gorrec F. Protein crystallization screens developed at the MRC laboratory of molecular biology. Drug Discov Today. 2016;21:819–825.
- Teplitsky E, Joshi K, Ericson DL, et al. High throughput screening using acoustic droplet ejection to combine protein crystals and chemical libraries on crystallization plates at high density. J Struct Biol. 2015;191:49–58.
- Stewart PS, Mueller-Dieckmann J. Automation in biological crystallization. Acta Crystallogr F Struct Biol Commun. 2014;70:686–696.
- Yin X, Scalia A, Leroy L, et al. Hitting the target: fragment screening with acoustic in situ co-crystallization of proteins plus fragment libraries on pin-mounted data-collection micromeshes. Acta Crystallogr D Biol Crystallogr. 2014;70:1177–1189.
- Dinc I, Pusey ML, Aygun RS. Optimizing associative experimental design for protein crystallization screening. IEEE Trans Nanobiosci. 2016;15:101–112.
- Wang H, Feng L, Zhang Z, et al. Crysalis: an integrated server for computational analysis and design of protein crystallization. Sci Rep. 2016;6:21383.
- Majorek KA, Kuhn ML, Chruszcz M, et al. Double trouble-buffer selection and his-tag presence may be responsible for nonreproducibility of biomedical experiments. Protein Sci. 2014;23:1359–1368.
- Altan I, Charbonneau P, Snell EH. Computational crystallization. Arch Biochem Biophys. 2016;602:12–20.