Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ab initio macromolecular phasing has been so far limited to small proteins diffracting at atomic resolution (beyond 1.2 A) unless heavy atoms are present. We describe a general ab initio phasing method for 2 A data, based on combination of localizing model fragments such as small a-helices with Phaser and density modification with SHELXE. We implemented this approach in the program Arcimboldo to solve a 222-amino-acid structure at 1.95 A.
Crystallographic ab initio protein structure solution below atomic resolution.,Rodriguez DD, Grosse C, Himmel S, Gonzalez C, de Ilarduya IM, Becker S, Sheldrick GM, Uson I Nat Methods. 2009 Sep;6(9):651-3. Epub 2009 Aug 16. PMID:19684596[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rodriguez DD, Grosse C, Himmel S, Gonzalez C, de Ilarduya IM, Becker S, Sheldrick GM, Uson I. Crystallographic ab initio protein structure solution below atomic resolution. Nat Methods. 2009 Sep;6(9):651-3. Epub 2009 Aug 16. PMID:19684596 doi:10.1038/nmeth.1365