Improvement of crystal quality for tetragonal hen egg white lysozyme crystals under application of an external alternating current electric field

2013 ◽  
Vol 46 (1) ◽  
pp. 25-29 ◽  
Author(s):  
H. Koizumi ◽  
S. Uda ◽  
K. Fujiwara ◽  
M. Tachibana ◽  
K. Kojima ◽  
...  

X-ray diffraction rocking-curve measurements were performed on tetragonal hen egg white lysozyme (HEWL) crystals grown with and without application of an external alternating current (AC) electric field, and then the crystal quality was assessed by the FWHMs of each rocking-curve profile. The FWHMs for HEWL crystals grown with an external electric field were smaller than those for crystals grown without. In particular, the average FWHM for the 12 12 0 reflection with an external electric field (0.0034°) was significantly smaller than that without (0.0061°). This indicates that the crystal quality of HEWL crystals was improved by application of the external AC electric field. This crystallization technique can be expected to enhance the resolution of protein molecule structure analysis by X-ray diffraction.

2007 ◽  
pp. 156-158 ◽  
Author(s):  
Angela Casini ◽  
Guido Mastrobuoni ◽  
Claudia Temperini ◽  
Chiara Gabbiani ◽  
Simona Francese ◽  
...  

2012 ◽  
Vol 45 (3) ◽  
pp. 517-522 ◽  
Author(s):  
Sebastian Send ◽  
Ali Abboud ◽  
Wolfram Leitenberger ◽  
Manfred S. Weiss ◽  
Robert Hartmann ◽  
...  

A crystal of hen egg-white lysozyme was analyzed by means of energy-dispersive X-ray Laue diffraction with white synchrotron radiation at 2.7 Å resolution using a pnCCD detector. From Laue spots measured in a single exposure of the arbitrarily oriented crystal, the lattice constants of the tetragonal unit cell could be extracted with an accuracy of about 2.5%. Scanning across the sample surface, Laue images with split reflections were recorded at various positions. The corresponding diffraction patterns were generated by two crystalline domains with a tilt of about 1° relative to each other. The obtained results demonstrate the potential of the pnCCD for fast X-ray screening of crystals of macromolecules or proteins prior to conventional X-ray structure analysis. The described experiment can be automatized to quantitatively characterize imperfect single crystals or polycrystals.


2014 ◽  
Vol 401 ◽  
pp. 238-241
Author(s):  
Kei Wako ◽  
Daiki Fujii ◽  
Shiro Tsukashima ◽  
Takeharu Kishi ◽  
Masaru Tachibana ◽  
...  

2012 ◽  
Vol 45 (5) ◽  
pp. 1009-1014 ◽  
Author(s):  
Kei Wako ◽  
Kunio Kimura ◽  
Yu Yamamoto ◽  
Takuya Sawaura ◽  
Mengyuan Shen ◽  
...  

Digital X-ray topography using an X-ray CCD camera and conventional X-ray topography using X-ray film were used to investigate tetragonal hen egg-white lysozyme (HEWL) crystals. Previously, clear dislocation images of protein crystals were mainly obtained by film methods. Earlier studies of HEWL crystals using an X-ray CCD camera mainly revealed domain structures. In the present study, dislocation images of the same HEWL crystal have been obtained by using conventional X-ray film and a digital X-ray CCD camera. The results demonstrate that digital topography using an X-ray CCD camera is an effective method for characterizing protein crystals. A series of digital topographic images were analyzed by the method developed by Lovelace, Murphy, Pahl, Brister & Borgstahl [J. Appl. Cryst.(2006),39, 425–432]. Sub-peaks and peak broadening originating from dislocations in local rocking curves were observed. Moreover, the crystal perfection was evaluated by mapping the angular positions of the maximums and the full widths at half-maximum of local rocking curves.


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