scholarly journals New protein crystallization device by counter-diffusion method andin situstructure determination

2007 ◽  
Vol 63 (a1) ◽  
pp. s137-s137
Author(s):  
T. Hasegawa ◽  
K. Hamada ◽  
M. Sato ◽  
M. Motohara ◽  
S. Sano ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
Diffusion Method ◽  
New Protein ◽  
Counter Diffusion

scholarly journals A numerical model of protein crystallization with counter diffusion method

2016 ◽  
Vol 741 ◽  
pp. 012053 ◽  
Author(s):  
A S Sokolovskiy ◽  
Yu V Trushin ◽  
M N Lubov ◽  
I E Eliseev ◽  
A N Yudenko ◽  
...  
Keyword(s):  
Numerical Model ◽  
Protein Crystallization ◽  
Diffusion Method ◽  
Counter Diffusion

A gradual desiccation method for improving the efficiency of protein crystallization screening

2012 ◽  
Vol 45 (4) ◽  
pp. 758-765 ◽  
Author(s):  
Qin-Qin Lu ◽  
Xu-Zhuo Xie ◽  
Rui-Qing Chen ◽  
Zi-Qing Wu ◽  
Qing-Di Cheng ◽  
...  
Keyword(s):  
Success Rate ◽  
Protein Crystallization ◽  
Diffusion Method ◽  
Powerful Method ◽  
Vapor Diffusion ◽  
Optimal Amount ◽  
Reservoir Solution ◽  
The One

In vapor diffusion protein crystallization screening, it has been reported that replacing the reservoir solution with desiccant can increase the crystallization success rate. Therefore, the desiccation method is a potentially powerful method in practical protein crystallization screening. However, this method is difficult to apply broadly because the optimal amount of desiccant for a specific screening task is unknown. Utilizing an unsuitable amount of desiccant can result in even worse screening results than would be obtained from the traditional vapor diffusion method. Here, it is shown that by employing a modified strategy, named the gradual desiccation method, the problem can be solved without knowing the optimal amount of desiccant, and the crystallization success rate can be further increased compared with the one-time desiccation method.

scholarly journals Crystallization and preliminary X-ray crystallographic analysis of Pz peptidase B fromGeobacillus collagenovoransMO-1

2012 ◽  
Vol 68 (7) ◽  
pp. 757-759 ◽  
Author(s):  
Hiroaki Nakano ◽  
Allin Hosokawa ◽  
Ryuji Tagawa ◽  
Koji Inaka ◽  
Kazunori Ohta ◽  
...  
Keyword(s):  
Space Station ◽  
Crystallographic Analysis ◽  
Diffusion Method ◽  
Unit Cell Parameters ◽  
Data Set ◽  
Peptide Substrates ◽  
X Ray ◽  
Cell Parameters ◽  
Experiment Module ◽  
Counter Diffusion

Pz peptidase B is an intracellular M3 metallopeptidase that is found together with Pz peptidase A in the thermophileGeobacillus collagenovoransMO-1 and recognizes collagen-specific tripeptide units (-Gly-Pro-X-). These peptidases have low homology in their primary structures; however, their cleavage patterns towards peptide substrates are similar. In this work, Pz peptidase B was crystallized using the counter-diffusion method. Data were collected to a resolution of 1.6 Å at 100 K from a crystal obtained in the Japanese Experiment Module (JEM; also known as `Kibo') at the International Space Station (ISS). The crystal belonged to the trigonal space groupP3121, with unit-cell parametersa=b= 87.64,c= 210.5 Å. A complete data set was also obtained from crystals of selenomethionine-substituted protein.

Efficient Screening Methodology for Protein Crystallization Based on the Counter-Diffusion Technique

2017 ◽  
Vol 17 (12) ◽  
pp. 6780-6786 ◽  
Author(s):  
Luis A. González-Ramírez ◽  
Carlos R. Ruiz-Martínez ◽  
Rafael A. Estremera-Andújar ◽  
Carlos A. Nieves-Marrero ◽  
Alfonso García-Caballero ◽  
...  
Keyword(s):  
Protein Crystallization ◽  
Diffusion Technique ◽  
Efficient Screening ◽  
Counter Diffusion

scholarly journals Effect of Temperature on Synthesis of ZIF-8 Membranes for Propylene/propane Separation by Counter Diffusion Method

2015 ◽  
Vol 58 (4) ◽  
pp. 237-244 ◽  
Author(s):  
Nobuo Hara ◽  
Miki Yoshimune ◽  
Hideyuki Negishi ◽  
Kenji Haraya ◽  
Shigeki Hara ◽  
...  
Keyword(s):  
Effect Of Temperature ◽  
Diffusion Method ◽  
Counter Diffusion

A simple and efficient innovation of the vapor-diffusion method for controlling nucleation and growth of large protein crystals

2001 ◽  
Vol 34 (3) ◽  
pp. 388-391 ◽  
Author(s):  
Genpei Li ◽  
Ye Xiang ◽  
Ying Zhang ◽  
Da-Cheng Wang
Keyword(s):  
Crystallization Process ◽  
Protein Crystallization ◽  
Protein Crystals ◽  
Diffusion Method ◽  
Capillary Barrier ◽  
Large Protein ◽  
Vapor Diffusion ◽  
Crystallization Experiments ◽  
Water Vaporization ◽  
Improved Technique

The rate of water vaporization in the vapor-diffusion method is critical for the protein crystallization process. Present methods, however, allow little or no control of the equilibration rates. This paper presents a relatively simple innovation of the conventional vapor-diffusion method by introducing a capillary barrier (for hanging drop) or a punched film barrier (for both hanging and sitting drop) between drop and reservoir, which can be beneficial in controlling the water vaporization rate, thereby promoting growth of large protein crystals. The crystallization experiments for lysozyme, trichosanthin and a novel neurotoxin BmK Mu9 show that this modified vapor-controlling-diffusion method is very effective for producing large protein crystals. The improved technique can be routinely used as a method for the preparation of other macromolecular and small-molecule crystals whose crystallization involves vaporization of water.

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