@article {9900,
	title = {Use of Gold Nanoparticles as Additives in Protein Crystallization},
	journal = {Crystal Growth \& Design},
	volume = {14},
	number = {1},
	year = {2014},
	note = {<p>ISI Document Delivery No.: 284RC Times Cited: 0 Cited Reference Count: 19 Ribeiro, Diana Kulakova, Alina Quaresma, Pedro Pereira, Eulalia Bonifacio, Cecilia Romao, Maria Joao Franco, Ricardo Carvalho, Ana Luisa Portuguese Science and Technology Foundation (FCT-MEC); COMPETE [PTDC/CTM-NAN/112241/2009, PEst-C/EQB/LA0006/2011, PEst-C/EQB/LA0006/2013] The authors would like to acknowledge Abhik Mukhopadhyay for assistance in data collection and processing of lysozyme crystals, Teresa Santos-Silva, Angelina Palma, Benedita Pinheiro, Marcia Correia, and Catarina Coelho for kindly providing the model proteins used as "real" cases in this study, and Marino Santos for data processing from albumin crystals and assistance in preparation of figures. We also acknowledge assistance in synchrotron data collection at ESRF (Grenoble, France) and SLS (Villigen, Switzerland). The work was supported by the Portuguese Science and Technology Foundation (FCT-MEC) and COMPETE through Grants PTDC/CTM-NAN/112241/2009 to R.F. and Grants PEst-C/EQB/LA0006/2011 and PEst-C/EQB/LA0006/2013 (to Associate Lab REQUIMTE). Amer chemical soc Washington</p>
},
	pages = {222-227},
	type = {Journal Article},
	abstract = {<p>Gold nanoparticles (AuNPs) exhibit unique properties that have made them a very attractive material for application in biological assays. Given the potentially interesting interactions between AuNPs and biological macromolecules, we investigated AuNPs-induced protein crystal growth. Differently functionalized AuNPs were tested as additives in cocrystallization studies with model proteins (hen egg white lysozyme (HEWL), ribonuclease A (RNase A), and proteinase K) as well as with case studies where there were problems in obtaining well-diffracting crystals. Trials were performed considering different crystallization drawbacks, from total absence of crystals to improvement of crystal morphology, size, twinning, and number of crystals per drop. Improvement of some of these factors was observed in the cases of HEWL, RNase A, phenylalanine hydroxylase (PAR), myoglobin, native aldehyde oxidase (AOH), and human albumin. In these proteins, the presence of the AuNPs promoted an increase in the size and/or better crystal morphology. From the systematic trials and subsequent observations, it can be concluded that the introduction of AuNPs should definitely be considered in crystal optimization trials to improve previously determined crystallization conditions.</p>
},
	keywords = {Chemistry Crystallography Materials Science},
	issn = {1528-7483},
	doi = {10.1021/cg4014398},
	url = {<Go to ISI>://WOS:000329337000029},
	author = {Ribeiro, D and Kulakova, A. and P. Quaresma and Pereira, E. and Bonifacio, C. and Romao, M. J. and Franco, R. and Carvalho, A. L.}
}
