Source:http://linkedlifedata.com/resource/pubmed/id/11526326
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 9
|
| pubmed:dateCreated |
2001-8-29
|
| pubmed:abstractText |
The truncated 1,3-1,4-beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase; E.C. 3.2.1.73) from Fibrobacter succinogenes was crystallized in four different forms by the vapour-diffusion method. Form A crystals have the largest trigonal P321 unit cell, diffracting to 3.0 A resolution with four to six molecules per asymmetric unit. Form B and C crystals belong to the same monoclinic space group P2(1), but the form B unit cell is twice as large as the unit cell of form C. Form B crystals diffract to 2.5 A resolution and contain four molecules per asymmetric unit. Form C crystals diffract to 2.1 A resolution and contain two molecules per asymmetric unit. Form D crystals have the smallest orthorhombic P2(1)2(1)2(1) unit cell, containing only one molecule per asymmetric unit, and diffract beyond 2.1 A resolution. The crystallization conditions for form B and C crystals are almost identical, except that form C crystals were grown in the presence of 2 mM Ca(2+) ions. It is likely that Ca(2+) directly binds to the glucanase, leading to unit-cell shrinkage as observed in other Bacillus glucanase crystals. A self-rotation search identified non-crystallographic twofold axes that combine with the crystallographic twofold dyads to give 222 symmetry for both form A and form B crystals, indicating that the glucanase has a tendency to pack in 222 symmetry.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0907-4449
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
57
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1303-6
|
| pubmed:dateRevised |
2007-7-24
|
| pubmed:meshHeading | |
| pubmed:year |
2001
|
| pubmed:articleTitle |
Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes.
|
| pubmed:affiliation |
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
|
| pubmed:publicationType |
Journal Article
|