Interfacial functional terminals enhance the heterogeneous nucleation of lysozyme crystals

CrystEngComm ◽  
2018 ◽  
Vol 20 (18) ◽  
pp. 2499-2510 ◽  
Author(s):  
Xinmeng Tong ◽  
Junjie Kang ◽  
Jinli Zhang ◽  
Xin Jia ◽  
Wei Li

A series of functional terminals were designed to interact with the flexible loop residues of lysozymes, aiming to produce quality protein crystalsviaintensified heterogeneous nucleation.

CrystEngComm ◽  
2019 ◽  
Vol 21 (12) ◽  
pp. 1992-2001 ◽  
Author(s):  
Xuechao Li ◽  
Han Liu ◽  
Xinmeng Tong ◽  
Sirui Dai ◽  
Jinli Zhang ◽  
...  

Charged polymers (PGA and PL) interact with lysozyme and then promote the heterogeneous nucleation of the crystals.


2021 ◽  
Vol 54 (1) ◽  
pp. 163-168
Author(s):  
Ryo Suzuki ◽  
Marina Abe ◽  
Kenichi Kojima ◽  
Masaru Tachibana

X-ray topography is a useful and nondestructive method for direct observation of crystal defects in nearly perfect single crystals. The grown-in dislocations from the cross-linked seed crystal in tetragonal hen egg-white lysozyme crystals were successfully characterized by digital X-ray topography. Digital X-ray topographs with various reflections were easily obtained by reconstruction of sequential rocking-curve images. The Burgers vector of the dislocation is different from those reported previously. Interestingly, one of the dislocations had a bent shape. The preferred direction of the dislocation line was analysed by the estimated dislocation energy based on the dislocation theory. The dislocation energy can be estimated by the dislocation theory even in protein crystals composed of macromolecules.


2018 ◽  
Vol 74 (12) ◽  
pp. 1200-1207 ◽  
Author(s):  
Jose A. Gavira ◽  
Mayte Conejero-Muriel ◽  
José Manuel Delgado-López

The fragility of protein crystals plays an important role in the final quality of the diffraction data and therefore that of the derived three-dimensional structural model. The growth of protein crystals in gels of various natures has been shown to overcome this problem, facilitating the manipulation of the crystals; this is probably owing, amongst other factors, to the incorporation of the gel fibres within the body of the crystal. In this study, lysozyme crystals were grown in silica gel at a wide range of concentrations of up to 22%(v/v) to quantitatively determine the amount of gel incorporated into the crystal structure by means of thermogravimetric analysis. The interaction between the silica fibres and the lysozyme molecules within the crystals was also investigated using Raman spectroscopy and the direct influence on the crystalline protein stability was analysed using differential scanning calorimetry. Finally, the benefits of the use of gel-grown crystals to overgrow protein crystals intended for neutron diffraction are highlighted.


2012 ◽  
Vol 22 (41) ◽  
pp. 21928 ◽  
Author(s):  
F. Kertis ◽  
S. Khurshid ◽  
O. Okman ◽  
J. W. Kysar ◽  
L. Govada ◽  
...  

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