scholarly journals Molecular Mechanism of Human Centromere Protein Function.

1993 ◽  
Vol 67 (11) ◽  
pp. 1555-1562
Author(s):  
Kenji SUGIMOTO
2002 ◽  
Vol 275 (1) ◽  
pp. 81-91 ◽  
Author(s):  
Kang Song ◽  
Bobbi Gronemeyer ◽  
Wei Lu ◽  
Emily Eugster ◽  
John E. Tomkiel

Genomics ◽  
1994 ◽  
Vol 24 (1) ◽  
pp. 187-188 ◽  
Author(s):  
Naohiko Seki ◽  
Toshiyuki Saito ◽  
Katsumi Kitagawa ◽  
Hiroshi Masumoto ◽  
Tuneko Okazaki ◽  
...  

Author(s):  
Yoshinao Muro ◽  
Yuta Yamashita ◽  
Haruka Koizumi ◽  
Takuya Takeichi ◽  
Masashi Akiyama

2014 ◽  
Vol 70 (a1) ◽  
pp. C614-C614
Author(s):  
Tobias Weinert ◽  
Sandro Waltersperger ◽  
Vincent Olieric ◽  
Federica Basilico ◽  
Valentina Cecatiello ◽  
...  

Up until now, comparatively few structures were solved by native SAD. Recent advances in multi crystal averaging [1] have shown that native SAD can be applied to an increasing number of cases. Though theoretically possible [2], successful structure solutions from twinned data have not been reported yet. Here, we report the structure solution of the human Centromere protein M from a merohedrally twinned crystal with a twinning fraction of 0.45 in the space group P3. The data were collected at the bending magnet beamline X06DA at the Swiss Light Source, which is equipped with the in-house developed multi-axis goniometer PRIGo and the PILATUS 2M detector. A highly redundant 2.2 Å dataset was collected in a number of different crystal orientations. A substructure solution could only be obtained after 50000 SHELXD [3] tries. Automatic model building after phasing and density modification resulted in a model with the majority of residues built correctly. We will present this particularly difficult case together with other more routine cases, all solved with the same experimental setup and at the beamline X06DA.


2021 ◽  
Vol 22 (14) ◽  
pp. 7267
Author(s):  
Léni Jodaitis ◽  
Thomas van Oene ◽  
Chloé Martens

Membrane proteins have evolved to work optimally within the complex environment of the biological membrane. Consequently, interactions with surrounding lipids are part of their molecular mechanism. Yet, the identification of lipid–protein interactions and the assessment of their molecular role is an experimental challenge. Recently, biophysical approaches have emerged that are compatible with the study of membrane proteins in an environment closer to the biological membrane. These novel approaches revealed specific mechanisms of regulation of membrane protein function. Lipids have been shown to play a role in oligomerization, conformational transitions or allosteric coupling. In this review, we summarize the recent biophysical approaches, or combination thereof, that allow to decipher the role of lipid–protein interactions in the mechanism of membrane proteins.


PLoS ONE ◽  
2011 ◽  
Vol 6 (3) ◽  
pp. e17151 ◽  
Author(s):  
Samantha G. Zeitlin ◽  
Brian R. Chapados ◽  
Norman M. Baker ◽  
Caroline Tai ◽  
Geir Slupphaug ◽  
...  

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