Corrigendum to “Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114” [J. Mol. Biol. 363 (2006) 161–173]

2007 ◽  
Vol 365 (3) ◽  
pp. 901
Author(s):  
Andrey Y. Kovalevsky ◽  
Fengling Liu ◽  
Sofiya Leshchenko ◽  
Arun K. Ghosh ◽  
John M. Louis ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Binding Sites ◽  
Hiv 1

scholarly journals Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114

2006 ◽  
Vol 363 (1) ◽  
pp. 161-173 ◽  
Author(s):  
Andrey Y. Kovalevsky ◽  
Fengling Liu ◽  
Sofiya Leshchenko ◽  
Arun K. Ghosh ◽  
John M. Louis ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Binding Sites ◽  
Hiv 1

scholarly journals A Novel Adenylate Binding Site Confers Phosphopantetheine Adenylyltransferase Interactions with Coenzyme A

2003 ◽  
Vol 185 (14) ◽  
pp. 4074-4080 ◽  
Author(s):  
Tina Izard
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Binding Site ◽  
Active Site ◽  
Binding Sites ◽  
Biosynthetic Pathway ◽  
Coenzyme A ◽  
Asymmetric Unit ◽  
Phosphate Moiety ◽  
Reversible Transfer

ABSTRACT Phosphopantetheine adenylyltransferase (PPAT) regulates the key penultimate step in the essential coenzyme A (CoA) biosynthetic pathway. PPAT catalyzes the reversible transfer of an adenylyl group from Mg2+:ATP to 4′-phosphopantetheine to form 3′-dephospho-CoA (dPCoA) and pyrophosphate. The high-resolution crystal structure of PPAT complexed with CoA has been determined. Remarkably, CoA and the product dPCoA bind to the active site in distinct ways. Although the phosphate moiety within the phosphopantetheine arm overlaps, the pantetheine arm binds to the same pocket in two distinct conformations, and the adenylyl moieties of these two ligands have distinct binding sites. Moreover, the PPAT:CoA crystal structure confirms the asymmetry of binding to the two trimers within the hexameric enzyme. Specifically, the pantetheine arm of CoA bound to one protomer within the asymmetric unit displays the dPCoA-like conformation with the adenylyl moiety disordered, whereas CoA binds the twofold-related protomer in an ordered and unique fashion.

High resolution STEM imaging study on high Tc superconductor YBa2CuaO7-x

1988 ◽  
Vol 46 ◽  
pp. 882-883
Author(s):  
H.-J. Ou ◽  
J. M. Cowley
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Grain Boundary ◽  
Strong Field ◽  
Imaging Study ◽  
Structure Defects ◽  
High Tc ◽  
High Tc Superconductor ◽  
Diffraction Patterns ◽  
Lattice Planes

Using the dedicate VG-HB5 STEM microscope, the crystal structure of high Tc superconductor of YBa2Cu3O7-x has been studied via high resolution STEM (HRSTEM) imaging and nanobeam (∽3A) diffraction patterns. Figure 1(a) and 2(a) illustrate the HRSTEM image taken at 10' times magnification along [001] direction and [100] direction, respectively. In figure 1(a), a grain boundary with strong field contrast is seen between two crystal regions A and B. The grain boundary appears to be parallel to a (110) plane, although it is not possible to determine [100] and [001] axes as it is in other regions which contain twin planes [3]. Following the horizontal lattice lines, from left to right across the grain boundary, a lattice bending of ∽4° is noticed. Three extra lattice planes, indicated by arrows, were found to terminate at the grain boundary and form dislocations. It is believed that due to different chemical composition, such structure defects occur during crystal growth. No bending is observed along the vertical lattice lines.

Perovskite Solar Cells: Crystal Structure and Interface Architecture with High Resolution TEM Observations

2017 ◽  
Author(s):  
Satoshi Uchida ◽  
Tae Woong Kim ◽  
Ludmila Cojocaru ◽  
Takashi Kondo ◽  
Hiroshi Segawa
Keyword(s):  
Crystal Structure ◽  
Solar Cells ◽  
High Resolution ◽  
Perovskite Solar Cells ◽  
High Resolution Tem

scholarly journals Improved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450

1996 ◽  
Vol 3 (4) ◽  
pp. 301-314 ◽  
Author(s):  
C. Nicholas Hodge ◽  
Paul E. Aldrich ◽  
Lee T. Bacheler ◽  
Chong-Hwan Chang ◽  
Charles J. Eyermann ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Human Pharmacokinetics ◽  
Resistance Profile ◽  
X Ray ◽  
Hiv 1
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