Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1990-4-10
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
211
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
297-9
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:2137884-Bacterial Outer Membrane Proteins,
pubmed-meshheading:2137884-Bacteriophage lambda,
pubmed-meshheading:2137884-Cell Fractionation,
pubmed-meshheading:2137884-Cell Membrane,
pubmed-meshheading:2137884-Crystallization,
pubmed-meshheading:2137884-Escherichia coli,
pubmed-meshheading:2137884-Porins,
pubmed-meshheading:2137884-Receptors, Virus,
pubmed-meshheading:2137884-X-Ray Diffraction
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Crystallization and preliminary X-ray characterization of maltoporin from Escherichia coli.
|
| pubmed:affiliation |
Department of Microbiology, University of Basel, Switzerland.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|