Crystallization and preliminary X-ray diffraction analysis of Langat virus envelope protein domain III.

نویسندگان

  • Mark A White
  • Deqian Liu
  • Michael R Holbrook
  • Robert E Shope
  • Alan D T Barrett
  • Robert O Fox
چکیده

The putative receptor-binding domain (domain III) of the flavivirus Langat envelope glycoprotein has been crystallized using the hanging-drop vapor-diffusion method at 277 K. Two distinct crystal morphologies were observed to grow under the same conditions. The crystal forms both belong to a trigonal space group, P3(1)21 or P3(2)21, with unit-cell parameters a = 80.93, c = 132.1 A and a = 104.8, c = 219.5 A for forms I and II, respectively. Complete data sets to 2.9 and 3.35 A, respectively, have been collected at 100 K with Cu Kalpha X-rays from a rotating-anode generator.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Dengue virus type-3 envelope protein domain III; expression and immunogenicity

Objective(s): Production of a recombinant and immunogenic antigen using dengue virus type-3 envelope protein is a key point in dengue vaccine development and diagnostic researches. The goals of this study were providing a recombinant protein from dengue virus type-3 envelope protein and evaluation of its immunogenicity in mice. Materials and Methods: Multiple amino acid sequences of different i...

متن کامل

Crystallization and preliminary X-ray diffraction studies of a surface mutant of the middle domain of PB2 from human influenza A (H1N1) virus.

In the last hundred years, four influenza pandemics have been experienced, beginning with that in Spain in 1918. Influenza A virus causes severe pneumonia and its RNA polymerase is an important target for drug design. The influenza A (H1N1) virus has eight ribonucleoprotein complexes, which are composed of viral RNA, RNA polymerases and nucleoproteins. PB2 forms part of the RNA polymerase compl...

متن کامل

Refolding, crystallization and preliminary X-ray structural studies of the West Nile virus envelope (E) protein domain III.

Domain III of the West Nile virus envelope protein, the putative receptor-binding domain, is a major virion-surface determinant for virulence. This protein was reported to be intrinsically unstable and has defied previous crystallization attempts. It has now been purified from inclusion bodies by protein refolding and was crystallized using the hanging-drop vapour-diffusion method at 291 K. The...

متن کامل

Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1

Tm-1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N-terminus and a TIM-barrel-like domain at its C-terminus. The N-terminal domain of Tm-1 has an inhibitory activity and its three-dimensional structure has not been determined. Here, the crystallization and preliminary X-ray diffraction of the N-terminal domain of ...

متن کامل

Expression, purification, crystallization and preliminary X-ray diffraction analysis of a mammalian type 10 adenylyl cyclase.

The second messenger cAMP is synthesized in mammals by ten differently regulated adenylyl cyclases (AC1-10). These ACs are grouped into nucleotidyl cyclase class III based on homologies in their catalytic domains. The catalytic domain of AC10 is unique, however, in being activated through direct interaction with calcium and bicarbonate. Here, the production, crystallization and X-ray diffractio...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Acta crystallographica. Section D, Biological crystallography

دوره 59 Pt 6  شماره 

صفحات  -

تاریخ انتشار 2003