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Title: Path to protein crystallization

Abstract

Growth of two-dimensional S-layer crystals on supported lipid bilayers observed in solution using in situ atomic force microscopy. This movie shows proteins sticking onto the supported lipid bilayer, forming a mobile phase that condenses into amorphous clusters, and undergoing a phase transition to crystalline clusters composed of 2 to 15 tetramers. These initial clusters then enter a growth phase in which new tetramers form exclusively at unoccupied lattice sites along the cluster edges.

Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1046971
Resource Type:
Multimedia
Country of Publication:
United States
Language:
English
Subject:
74 ATOMIC AND MOLECULAR PHYSICS; 77 NANOSCIENCE AND NANOTECHNOLOGY; LBNL; CRYSTALS; CRYSTALLINE CLUSTERS; ATOMIC FORCE MICROSCOPY; PROTEINS; PHASES

Citation Formats

None. Path to protein crystallization. United States: N. p., 2010. Web.
None. Path to protein crystallization. United States.
None. Fri . "Path to protein crystallization". United States. https://www.osti.gov/servlets/purl/1046971.
@article{osti_1046971,
title = {Path to protein crystallization},
author = {None},
abstractNote = {Growth of two-dimensional S-layer crystals on supported lipid bilayers observed in solution using in situ atomic force microscopy. This movie shows proteins sticking onto the supported lipid bilayer, forming a mobile phase that condenses into amorphous clusters, and undergoing a phase transition to crystalline clusters composed of 2 to 15 tetramers. These initial clusters then enter a growth phase in which new tetramers form exclusively at unoccupied lattice sites along the cluster edges.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2010},
month = {1}
}

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