| dc.contributor.author |
Bethanis, K |
en |
| dc.contributor.author |
Tzamalis, P |
en |
| dc.contributor.author |
Hountas, A |
en |
| dc.contributor.author |
Mishnev, AF |
en |
| dc.contributor.author |
Tsoucaris, G |
en |
| dc.date.accessioned |
2014-06-06T06:44:21Z |
|
| dc.date.available |
2014-06-06T06:44:21Z |
|
| dc.date.issued |
2000 |
en |
| dc.identifier.issn |
01087673 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1107/S0108767399013355 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/1829 |
|
| dc.subject.other |
calponin |
en |
| dc.subject.other |
ribonuclease |
en |
| dc.subject.other |
algorithm |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
Aspergillus |
en |
| dc.subject.other |
crystal structure |
en |
| dc.subject.other |
crystallography |
en |
| dc.subject.other |
entropy |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
protein structure |
en |
| dc.subject.other |
structure analysis |
en |
| dc.subject.other |
Algorithms |
en |
| dc.subject.other |
Crystallography, X-Ray |
en |
| dc.subject.other |
Protein Conformation |
en |
| dc.subject.other |
Proteins |
en |
| dc.subject.other |
Thermodynamics |
en |
| dc.subject.other |
Aspergillus |
en |
| dc.title |
Upgrading the twin variables algorithm for large structures |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1107/S0108767399013355 |
en |
| heal.publicationDate |
2000 |
en |
| heal.abstract |
Phase extension from lower to higher resolution by using an upgraded TWIN variables algorithm [Hountas & Tsoucaris (1995). Acta Cryst. A51, 754-763] in protein molecules with close to 1000 non-H atoms is presented. Three points of this procedure are of particular interest. (i) The use of a set of auxiliary variables providing a satisfactory fit for many kinds of constraints: the new algorithm works efficiently despite the extreme 'dilution' of very limited initial phase information into a much larger set of auxiliary variables. (ii) The extension of this auxiliary variables set beyond the resolution of the observed data, which enhances the phase extension in a so-called 'super-resolution' sphere. (iii) The use of the crystallographic symmetry as a new figure of merit and as a reliable test for the correctness of the phase-extension process allows an efficient screening. |
en |
| heal.journalName |
Acta Crystallographica Section A: Foundations of Crystallography |
en |
| dc.identifier.issue |
2 |
en |
| dc.identifier.volume |
56 |
en |
| dc.identifier.doi |
10.1107/S0108767399013355 |
en |
| dc.identifier.spage |
105 |
en |
| dc.identifier.epage |
111 |
en |