skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: High-throughput method for optimum solubility screening for homogeneity and crystallization of proteins

Abstract

An optimum solubility screen in which a panel of buffers and many additives are provided in order to obtain the most homogeneous and monodisperse protein condition for protein crystallization. The present methods are useful for proteins that aggregate and cannot be concentrated prior to setting up crystallization screens. A high-throughput method using the hanging-drop method and vapor diffusion equilibrium and a panel of twenty-four buffers is further provided. Using the present methods, 14 poorly behaving proteins have been screened, resulting in 11 of the proteins having highly improved dynamic light scattering results allowing concentration of the proteins, and 9 were crystallized.

Inventors:
 [1];  [1];  [2]
  1. Moraga, CA
  2. Walnut Creek, CA
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1034608
Patent Number(s):
8,105,983
Application Number:
11/393,209
Assignee:
The Regents of the University of California (Oakland, CA)
DOE Contract Number:  
AC02-05CH11231
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Kim, Sung-Hou, Kim, Rosalind, and Jancarik, Jamila. High-throughput method for optimum solubility screening for homogeneity and crystallization of proteins. United States: N. p., 2012. Web.
Kim, Sung-Hou, Kim, Rosalind, & Jancarik, Jamila. High-throughput method for optimum solubility screening for homogeneity and crystallization of proteins. United States.
Kim, Sung-Hou, Kim, Rosalind, and Jancarik, Jamila. Tue . "High-throughput method for optimum solubility screening for homogeneity and crystallization of proteins". United States. https://www.osti.gov/servlets/purl/1034608.
@article{osti_1034608,
title = {High-throughput method for optimum solubility screening for homogeneity and crystallization of proteins},
author = {Kim, Sung-Hou and Kim, Rosalind and Jancarik, Jamila},
abstractNote = {An optimum solubility screen in which a panel of buffers and many additives are provided in order to obtain the most homogeneous and monodisperse protein condition for protein crystallization. The present methods are useful for proteins that aggregate and cannot be concentrated prior to setting up crystallization screens. A high-throughput method using the hanging-drop method and vapor diffusion equilibrium and a panel of twenty-four buffers is further provided. Using the present methods, 14 poorly behaving proteins have been screened, resulting in 11 of the proteins having highly improved dynamic light scattering results allowing concentration of the proteins, and 9 were crystallized.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2012},
month = {1}
}

Patent:

Save / Share:

Works referenced in this record:

Sparse matrix sampling: a screening method for crystallization of proteins
journal, August 1991


Crystallizing proteins – a rational approach?
journal, July 1994


Light scattering of proteins as a criterion for crystallization
journal, August 1992


Dynamic light-scattering analysis of full-length human RPA14/32 dimer: purification, crystallization and self-association
journal, February 2001

  • Habel, Jeff E.; Ohren, Jeffrey F.; Borgstahl, Gloria E. O.
  • Acta Crystallographica Section D Biological Crystallography, Vol. 57, Issue 2
  • DOI: 10.1107/S0907444900015225

A preliminary solubility screen used to improve crystallization trials: crystallization and preliminary X-ray structure determination of Aeropyrum pernix flap endonuclease-1
journal, August 2004

  • Collins, Brandon K.; Tomanicek, Stephen J.; Lyamicheva, Natasha
  • Acta Crystallographica Section D Biological Crystallography, Vol. 60, Issue 9, p. 1674-1678
  • DOI: 10.1107/S090744490401844X