Literature DB >> 8742725

A brief description of I.C.E.: the integrated crystallographic environment.

S Hardt1, B Wang, M F Schmid.   

Abstract

We describe the current status of the program I.C.E., the Integrated Crystallographic Environment. I.C.E. is a windows-based, menu-driven image processing package mainly aimed toward crystallographic image processing, although some of its functions have been used in analyzing single particle data and helical objects. The system can take individual images of crystals through the entire process of data analysis, from windowing the raw image through to the final evaluation of defocus, symmetry and creation of projection reconstructions. Current plans are to incorporate a three-dimensional database of images and electron diffraction patterns, and 3-D merging and visualization.

Mesh:

Year:  1996        PMID: 8742725     DOI: 10.1006/jsbi.1996.0012

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  14 in total

1.  Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2.

Authors:  T Wendt; D Taylor; K M Trybus; K Taylor
Journal:  Proc Natl Acad Sci U S A       Date:  2001-04-03       Impact factor: 11.205

2.  Two-dimensional crystallization on lipid monolayers and three-dimensional structure of sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus.

Authors:  J Martín-Benito; F Gavilanes; V de Los Ríos; J M Mancheño; J J Fernández; J G Gavilanes
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

3.  Two-dimensional crystal structures of protein kinase C-delta, its regulatory domain, and the enzyme complexed with myelin basic protein.

Authors:  Alexander S Solodukhin; Heather L Caldwell; Julianne J Sando; Robert H Kretsinger
Journal:  Biophys J       Date:  2002-05       Impact factor: 4.033

4.  Phosphorylated smooth muscle heavy meromyosin shows an open conformation linked to activation.

Authors:  Bruce A J Baumann; Dianne W Taylor; Zhong Huang; Florence Tama; Patricia M Fagnant; Kathleen M Trybus; Kenneth A Taylor
Journal:  J Mol Biol       Date:  2011-11-04       Impact factor: 5.469

5.  The vacuolating toxin from Helicobacter pylori forms hexameric pores in lipid bilayers at low pH.

Authors:  D M Czajkowsky; H Iwamoto; T L Cover; Z Shao
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-02       Impact factor: 11.205

6.  Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments.

Authors:  Sonia Huecas; Oscar Llorca; Jasminka Boskovic; Jaime Martín-Benito; José María Valpuesta; José Manuel Andreu
Journal:  Biophys J       Date:  2007-11-16       Impact factor: 4.033

7.  Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging.

Authors:  Z H Zhou; S J Macnab; J Jakana; L R Scott; W Chiu; F J Rixon
Journal:  Proc Natl Acad Sci U S A       Date:  1998-03-17       Impact factor: 11.205

8.  Electron crystallographic analysis of two-dimensional streptavidin crystals coordinated to metal-chelated lipid monolayers.

Authors:  W Frey; J Brink; W R Schief; W Chiu; V Vogel
Journal:  Biophys J       Date:  1998-05       Impact factor: 4.033

9.  Assembly of retrovirus capsid-nucleocapsid proteins in the presence of membranes or RNA.

Authors:  G Zuber; J McDermott; S Karanjia; W Zhao; M F Schmid; E Barklis
Journal:  J Virol       Date:  2000-08       Impact factor: 5.103

10.  Characterization of Rous sarcoma virus Gag particles assembled in vitro.

Authors:  F Yu; S M Joshi; Y M Ma; R L Kingston; M N Simon; V M Vogt
Journal:  J Virol       Date:  2001-03       Impact factor: 5.103

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