Direct and Noninvasive Observation of Two-Dimensional Nucleation Behavior of Protein Crystals by Advanced Optical Microscopy

2007 ◽  
Vol 7 (10) ◽  
pp. 1980-1987 ◽  
Author(s):  
Alexander E. S. Van Driessche ◽  
Gen Sazaki ◽  
Fermín Otálora ◽  
Francisco M. González-Rico ◽  
Peter Dold ◽  
...  
Keyword(s):  
Optical Microscopy ◽  
Protein Crystals ◽  
Two Dimensional ◽  
Nucleation Behavior

[11] Two-dimensional protein crystals in aid of three-dimensional protein crystal growth

1997 ◽  
pp. 166-171
Author(s):  
Aled M. Edwards ◽  
Seth A. Darst ◽  
Sally A. Hemming ◽  
Francisco J. Asturias ◽  
Peter R. David ◽  
...  
Keyword(s):  
Crystal Growth ◽  
Three Dimensional ◽  
Protein Crystal ◽  
Protein Crystals ◽  
Two Dimensional ◽  
Protein Crystal Growth

Near-field optical microscopy of two-dimensional photonic and plasmonic crystals

1999 ◽  
Vol 59 (3) ◽  
pp. 2454-2460 ◽  
Author(s):  
Igor I. Smolyaninov ◽  
Walid Atia ◽  
Christopher C. Davis
Keyword(s):  
Optical Microscopy ◽  
Near Field ◽  
Two Dimensional ◽  
Plasmonic Crystals

Dendritic growth of two-dimensional protein crystals

Langmuir ◽  
1992 ◽  
Vol 8 (10) ◽  
pp. 2357-2360 ◽  
Author(s):  
Andrew C. Ku ◽  
Seth A. Darst ◽  
Roger D. Kornberg ◽  
Channing R. Robertson ◽  
Alice P. Gast
Keyword(s):  
Dendritic Growth ◽  
Protein Crystals ◽  
Two Dimensional

scholarly journals Optical mapping of the boundary of a two-dimensional electron gas by a nearfield optical microscopy

2010 ◽  
Vol 3 (2) ◽  
pp. 1171-1175 ◽  
Author(s):  
H. Ito ◽  
Y. Shibata ◽  
K. Furuya ◽  
S. Kashiwaya ◽  
Y. Ootuka ◽  
...  
Keyword(s):  
Optical Microscopy ◽  
Optical Mapping ◽  
Electron Gas ◽  
Two Dimensional ◽  
Dimensional Electron ◽  
Two Dimensional Electron Gas ◽  
Dimensional Electron Gas

scholarly journals Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals

IUCrJ ◽  
2019 ◽  
Vol 6 (1) ◽  
pp. 34-45 ◽  
Author(s):  
Cecilia M. Casadei ◽  
Karol Nass ◽  
Anton Barty ◽  
Mark S. Hunter ◽  
Celestino Padeste ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Diffraction Data ◽  
Structure Factor ◽  
Large Scale ◽  
Reciprocal Space ◽  
Protein Crystals ◽  
Two Dimensional ◽  
Data Set ◽  
Redundant Data ◽  
Serial Femtosecond Crystallography

Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments.

Study on variable nucleation efficiency of N,N ′-Dicyclohexyl-2,6-naphthalenedicarboxamide on isotactic polypropylene

2016 ◽  
Vol 29 (12) ◽  
pp. 1667-1679 ◽  
Author(s):  
Yaoqi Shi ◽  
Zhong Xin
Keyword(s):  
Optical Microscopy ◽  
Isotactic Polypropylene ◽  
Nucleating Agent ◽  
Recrystallization Process ◽  
Schematic Diagram ◽  
Microscopy Observation ◽  
Crystallization Peak ◽  
Nucleation Behavior ◽  
Polarized Optical Microscopy ◽  
Whole Process

N, N′-Dicyclohexyl-2,6-naphthalenedicarboxamide (NU100), a commercial β-nucleating agent (NA) for isotactic polypropylene (iPP), is found dissolvable in iPP melt. Various heating temperatures ( Ths) of iPP/NU100 cause different solubilities of NA, resulting in various aggregation morphologies of NU100 in the melt. Moreover, nucleation efficiency of NA NU100 on iPP changes with the Th of iPP/NU100. In this article, the effects of Th on nucleation behaviors of iPP nucleated with different concentrations of NU100 were systematically studied. The results indicated nucleation efficiency of NU100 depended not only on concentration of NA but also on Th of nucleated iPP. With the increase of Th, crystallization peak temperature ( Tcp) of nucleated iPP decreased remarkably. The whole process that Tcp shifted from 126.8°C to 120.8°C was obtained by investigating the nucleation behavior of iPP/0.1 wt% NU100. Polarized optical microscopy observation confirmed lower Tcp, representing the crystallization of iPP nucleated by dissolved–recrystallized NA NU100. Further, diverse aggregation morphologies of NA in iPP melt during crystallization were observed. A schematic diagram was proposed illustrating the morphologies formed during recrystallization process of NU100 melted at different Ths.

Application potentials of two dimensional protein crystals

1989 ◽  
Vol 9 (1-4) ◽  
pp. 13-20 ◽  
Author(s):  
Uwe B. Sleytr ◽  
Margit Sara ◽  
Dietmar Pum
Keyword(s):  
Protein Crystals ◽  
Two Dimensional
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