scholarly journals Time-Resolved X-ray Crystal Structure Analysis of Proteins.

1995 ◽  
Vol 35 (6) ◽  
pp. 245-248
Author(s):  
Shin-ichi ADACHI ◽  
Nobuhisa WATANABE

Cryoenzymological techniques provide a means of initiating enzymatic reactions in crystals homogeneously and of prolonging the lifetimes of intermediate reaction steps. Catalytic intermediates may accumulate to sufficiently high population for X-ray crystal structure analysis by time-resolved monochromatic or Laue diffraction data collection using synchrotron radiation. Due to short exposure times, intermediates may be studied at moderately low temperatures. A combination of cryoenzymology and time-resolved crystallography has been applied to crystal structure analysis at high resolution of an acyl-enzyme intermediate of a productive reaction catalysed by porcine pancreatic elastase.


RSC Advances ◽  
2013 ◽  
Vol 3 (37) ◽  
pp. 16313 ◽  
Author(s):  
Manabu Hoshino ◽  
Shunsuke Nozawa ◽  
Tokushi Sato ◽  
Ayana Tomita ◽  
Shin-ichi Adachi ◽  
...  

1999 ◽  
Vol 23 (9) ◽  
pp. 578-579
Author(s):  
Rainer Schobert ◽  
Hermann Pfab ◽  
Jutta Böhmer ◽  
Frank Hampel ◽  
Andreas Werner

Racemates of (η3-allyl)tricarbonyliron lactone complex Fe(CO)3{η1:η3-C(O)XCH2CHCMeCH2} 1a (X = O) and (η3-allyl)tricarbonyliron lactam complex 2a (X = NMe) are resolved on a preparative scale by HPLC on cellulose tris(3,5-dimethylphenyl)carbamate/silica gel RP-8 and the absolute configuration of (-)-2a is determined by X-ray crystal structure analysis.


2005 ◽  
Vol 88 (4) ◽  
pp. 731-750 ◽  
Author(s):  
Stefan Sahli ◽  
Brian Frank ◽  
W. Bernd Schweizer ◽  
François Diederich ◽  
Denise Blum-Kaelin ◽  
...  

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