Molecular and crystal structure of 1,4-diacethoxy naphthalene: Structural analysis of methyl substituted 1,4-diacethoxynaphthalenes

1989 ◽  
Vol 19 (2) ◽  
pp. 307-316
Author(s):  
Jos� Gonzalo Rodr�guez ◽  
Alfonso Pablo ◽  
Julian Lopez Lerma ◽  
Aurea Perales
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Molecular And Crystal Structure

scholarly journals Molekül- und Kristallstruktur von 1.1-Dimethylsilylentitanocendichlorid, (CH3)2Si(C5H4)2TiCl2 / Molecular and Crystal Structure of l,r-Dimethylsilylene Titanocene Dichloride, (CH3)2Si(C5H4)2TiCl2

1981 ◽  
Vol 36 (10) ◽  
pp. 1208-1210 ◽  
Author(s):  
Hartmut Köpf ◽  
Joachim Pickardt
Keyword(s):  
Molecular Structure ◽  
Crystal Structure ◽  
Structure Determination ◽  
Titanocene Dichloride ◽  
Molecular And Crystal Structure ◽  
Monoclinic Space Group ◽  
Crystal Data ◽  
Space Group ◽  
X Ray ◽  
Structural Dimensions

Abstract The molecular structure of the bridged [1]-titanocenophane 1,1'-dimethylsilylene titanocene dichloride, (CH3)2Si(C5H4)2TiCl2, has been investigated by an X-ray structure determination. Crystal data: monoclinic, space group C2/c, Z = 4, a = 1332.9(3), 6 = 988.7(3), c = 1068.9(3) pm, β = 113.43(2)°. The results are compared with the structural dimensions of similar compounds: 1,1'-methylene titanocene dichloride, CH2(C5H4)TiCl2, with the unbridged titanocene dichloride, (C5H5)2TiCl2 and the ethylene-bridged compound (CH2)2(C5H4)2TiCl2

scholarly journals Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate

2015 ◽  
Vol 71 (2) ◽  
pp. 199-205 ◽  
Author(s):  
George T. Lountos ◽  
Scott Cherry ◽  
Joseph E. Tropea ◽  
David S. Waugh
Keyword(s):  
Crystal Structure ◽  
Structural Analysis ◽  
Phosphatase Activity ◽  
Small Molecule ◽  
Molecular Basis ◽  
Protein Tyrosine Phosphatases ◽  
Simple Method ◽  
Dual Specificity Phosphatase ◽  
Dual Specificity ◽  
Nitrophenyl Phosphate

4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.

Products of the pyrolysis of [Os3(CO)11{P(OMe)3}]; the molecular and crystal structure of [Os5C(CO)13H{OP(OMe)2}{P(OMe)3}]

1981 ◽  
pp. 2250 ◽  
Author(s):  
Juan M. Fernandez ◽  
Brian F. G. Johnson ◽  
Jack Lewis ◽  
Paul R. Raithby
Keyword(s):  
Crystal Structure ◽  
Molecular And Crystal Structure
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