Literature DB >> 2137884

Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli.

K A Stauffer1, M G Page, A Hardmeyer, T A Keller, R A Pauptit.   

Abstract

Crystals of maltoporin (the bacteriophage lambda receptor of Escherichia coli) that diffract X-rays to 3 A resolution can be grown reproducibly. Maltoporin is an integral membrane protein, which forms a channel in the E. coli outer membrane that specifically facilitates the diffusion of maltose and maltodextrins. The crystals have a rhombic prismatic habit and belong to the orthorhombic space group C222(1) with unit cell dimensions a = 130 A, b = 213 A and c = 216 A. X-ray structure determination is underway.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 2137884     DOI: 10.1016/0022-2836(90)90351-L

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  4 in total

1.  Introduction: crystallization of membrane proteins--in need of a new focus?

Authors:  J M Sowadski
Journal:  J Bioenerg Biomembr       Date:  1996-02       Impact factor: 2.945

2.  Crystallization of Escherichia coli maltoporin in the trigonal space group R3.

Authors:  Mickael Blaise; Søren Thirup
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-12-23

3.  Prediction of membrane-spanning beta-strands and its application to maltoporin.

Authors:  T Schirmer; S W Cowan
Journal:  Protein Sci       Date:  1993-08       Impact factor: 6.725

4.  Overexpression of outer membrane porins in E. coli using pBluescript-derived vectors.

Authors:  R Ghosh; M Steiert; A Hardmeyer; Y F Wang; J P Rosenbusch
Journal:  Gene Expr       Date:  1998
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.