Two−dimensional protein crystals as patterning elements in molecular nanotechnology

1992 ◽  
Author(s):  
U. B. Sleytr ◽  
D. Pum ◽  
M. Sára ◽  
P. Messner
Keyword(s):  
Protein Crystals ◽  
Two Dimensional ◽  
Molecular Nanotechnology

[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

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

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 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.

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

scholarly journals Femtosecond X-ray diffraction from two-dimensional protein crystals

IUCrJ ◽  
2014 ◽  
Vol 1 (2) ◽  
pp. 95-100 ◽  
Author(s):  
Matthias Frank ◽  
David B. Carlson ◽  
Mark S. Hunter ◽  
Garth J. Williams ◽  
Marc Messerschmidt ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Bragg Diffraction ◽  
Protein Crystal ◽  
Protein Crystals ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray ◽  
Linac Coherent Light Source ◽  
Diffraction Patterns ◽  
Better Than

X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.

A novel free-mounting system for protein crystals: transformation and improvement of diffraction power by accurately controlled humidity changes

2000 ◽  
Vol 33 (5) ◽  
pp. 1223-1230 ◽  
Author(s):  
Reiner Kiefersauer ◽  
Manuel E. Than ◽  
Holger Dobbek ◽  
Lothar Gremer ◽  
Marcos Melero ◽  
...  
Keyword(s):  
Ccd Camera ◽  
Protein Crystals ◽  
Two Dimensional ◽  
Optical Analysis ◽  
Anaerobic Conditions ◽  
Volatile Substances ◽  
Video System ◽  
Novel Device ◽  
Free Gases

A novel device for capillary-free mounting of protein crystals is described. A controlled stream of air allows an accurate adjustment of the humidity at the crystal. The crystal is held on the tip of a micropipette. With a video system (CCD camera), the two-dimensional shadow projections of crystals can be recorded for optical analysis. Instead of the micropipette, a standard loop can also be used. Experiments and results for different crystal systems demonstrate the use of this method, also in combination with shock-freezing, to improve crystal order. Working with oxygen-free gases offers the possibility of crystal measurements under anaerobic conditions. Furthermore, the controlled application of arbitrary volatile substances with the gas stream is practicable.

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