The phase diagram of globular protein solutions : the role of the range of interaction

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Physics, 1998.Vita.Includes bibliographical references (p. 139-145).by Neer Ruben Asherie.Ph.D

Automating the application of smart materials for protein crystallization

The fabrication and validation of the first semi-liquid nonprotein nucleating agent to be administered automatically to crystallization trials is reported. This research builds upon prior demonstration of the suitability of molecularly imprinted polymers (MIPs; known as 'smart materials') for inducing protein crystal growth. Modified MIPs of altered texture suitable for high-throughput trials are demonstrated to improve crystal quality and to increase the probability of success when screening for suitable crystallization conditions. The application of these materials is simple, time-efficient and will provide a potent tool for structural biologists embarking on crystallization trials. © 2015, IUCR. All rights reserved

Design rules for the self-assembly of a protein crystal

Theories of protein crystallization based on spheres that form close-packed crystals predict optimal assembly within a `slot' of second virial coefficients and enhanced assembly near the metastable liquid-vapor critical point. However, most protein crystals are open structures stabilized by anisotropic interactions. Here, we use theory and simulation to show that assembly of one such structure is not predicted by the second virial coefficient or enhanced by the critical point. Instead, good assembly requires that the thermodynamic driving force be on the order of the thermal energy and that interactions be made as nonspecific as possible without promoting liquid-vapor phase separation.Comment: 5 pages, 4 figure

Protein crystallization in short-peptide supramolecular hydrogels: A versatile strategy towards biotechnological composite materials

Protein crystallization in hydrogels has been explored with the main purpose of facilitating the growth of high quality crystals while increasing their size to enhance their manipulation. New avenues are currently being built for the use of protein crystals as source materials to create sensors and drug delivery vehicles, to name just a few. In this sense, short-peptide supramolecular hydrogels may play a crucial role in integrating protein crystals within a wider range of applications. In this article, we show that protein crystallization in short-peptide supramolecular hydrogels is feasible and independent of the type of peptide that forms the hydrogel and/or the protein, although the output is not always the same. As a general trend, it is confirmed that hydrogel fibers are always incorporated within crystals so that novel composite materials for biotechnological applications with enhanced properties are produced.This research was funded by the MICINN (Spain) projects BIO2010-6800 (JAG), CTQ2012-34778 (JJDM), and “Factoría Española de Cristalización” Consolider-Ingenio 2010 (JAG & MCM), and by Junta de Andalucía (Spain) project P12-FQM- 2721 (LAC). EDRF funds JAG, LAC & JMC. JJDM thanks MICINN for a Ramon y Cajal Fellowship and MCM thanks CSIC for her JAE Fellowshi

Improved Success of Sparse Matrix Protein Crystallization Screening with Heterogeneous Nucleating Agents

Crystallization is a major bottleneck in the process of macromolecular structure determination by X-ray crystallography. Successful crystallization requires the formation of nuclei and their subsequent growth to crystals of suitable size. Crystal growth generally occurs spontaneously in a supersaturated solution as a result of homogenous nucleation. However, in a typical sparse matrix screening experiment, precipitant and protein concentration are not sampled extensively, and supersaturation conditions suitable for nucleation are often missed

Plasma Dynamics

Contains table of contents for Section 2 and reports on three research projects.National Science Foundation Grant ECS 89-02990U.S. Air Force - Office of Scientific Research Grant F49620-93-1-0108U.S. Army - Harry Diamond Laboratories Contract DAAL02-92-K-0037U.S. Department of Energy Grant DE-FG02-91-ER-40648U.S. Navy - Office of Naval Research Grant N00014-90-J-4130National Aeronautics and Space Administration Grant NAGW-2048National Science Foundation Grant ECS 88-22475U.S. Department of Energy Grant DE-FG02-91-ER-54109Magnetic Fusion Science Fellowship Progra

Heterogeneous Nucleation of Protein Crystals on Fluorinated Layered Silicate

Here, we describe an improved system for protein crystallization based on heterogeneous nucleation using fluorinated layered silicate. In addition, we also investigated the mechanism of nucleation on the silicate surface. Crystallization of lysozyme using silicates with different chemical compositions indicated that fluorosilicates promoted nucleation whereas the silicates without fluorine did not. The use of synthesized saponites for lysozyme crystallization confirmed that the substitution of hydroxyl groups contained in the lamellae structure for fluorine atoms is responsible for the nucleation-inducing property of the nucleant. Crystallization of twelve proteins with a wide range of pI values revealed that the nucleation promoting effect of the saponites tended to increase with increased substitution rate. Furthermore, the saponite with the highest fluorine content promoted nucleation in all the test proteins regardless of their overall net charge. Adsorption experiments of proteins on the saponites confirmed that the density of adsorbed molecules increased according to the substitution rate, thereby explaining the heterogeneous nucleation on the silicate surface

Plasma Dynamics

Contains table of contents for Section 2 and reports on four research projects.National Science Foundation Grant ECS-89-02990U.S. Air Force - Office of Scientific Research Grant AFOSR 89-0082-CU.S. Army - Harry Diamond Laboratories Contract DAAL02-89-K-0084U.S. Army - Harry Diamond Laboratories Contract DAAL02-92-K-0037U.S. Department of Energy Contract DE-AC02-90ER-40591U.S. Navy - Office of Naval Research Grant N00014-90-J-4130Lawrence Livermore National Laboratories Subcontract B-160456National Aeronautics and Space Administration Grant NAGW-2048National Science Foundation Grant ECS-88-22475U.S. Department of Energy Grant DE-FG02-91-ER-5410