about
Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontisThe crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdownCo-translational capturing of nascent ribosomal proteins by their dedicated chaperonesPHF13 is a molecular reader and transcriptional co-regulator of H3K4me2/3Structure of a 13-fold superhelix (almost) determined from first principles.Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models.Routine phasing of coiled-coil protein crystal structures with AMPLEInitiating heavy-atom-based phasing by multi-dimensional molecular replacementResidue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain.Macromolecular ab initio phasing enforcing secondary and tertiary structureStructure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB.ARCIMBOLDO_LITE: single-workstation implementation and use.Combining phase information in reciprocal space for molecular replacement with partial models.Structure and mechanism of a bacterial host-protein citrullinating virulence factor, Porphyromonas gingivalis peptidylarginine deiminaseStructural insights into the bacterial carbon-phosphorus lyase machineryRapid cadmium SAD phasing at the standard wavelength (1 Å).Experimental Phasing: Substructure Solution and Density Modification as Implemented in SHELX.Ab initio solution of macromolecular crystal structures without direct methodsGranular clustering of de novo protein models.Molecular symmetry-constrained systematic search approach to structure solution of the coiled-coil SRGAP2 F-BARx domain.The Structure of a Novel Thermophilic Esterase from the Planctomycetes Species, Thermogutta terrifontis Reveals an Open Active Site Due to a Minimal 'Cap' Domain.Structure solution with ARCIMBOLDO using fragments derived from distant homology models.Approaches to ab initio molecular replacement of α-helical transmembrane proteins.Recent developments in MrBUMP: better search-model preparation, graphical interaction with search models, and solution improvement and assessment.An introduction to experimental phasing of macromolecules illustrated by SHELX; new autotracing features.Fragon: rapid high-resolution structure determination from ideal protein fragments.ARCIMBOLDO on coiled coils.Ensembles generated from crystal structures of single distant homologues solve challenging molecular-replacement cases in AMPLE.X-ray and UV radiation-damage-induced phasing using synchrotron serial crystallography.The structure of a calcium-dependent phosphoinositide-specific phospholipase C fromPseudomonassp. 62186, the first from a Gram-negative bacteriumSIMBAD: a sequence-independent molecular-replacement pipeline
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Extending molecular-replacement solutions with SHELXE.
@en
Extending molecular-replacement solutions with SHELXE.
@nl
type
label
Extending molecular-replacement solutions with SHELXE.
@en
Extending molecular-replacement solutions with SHELXE.
@nl
prefLabel
Extending molecular-replacement solutions with SHELXE.
@en
Extending molecular-replacement solutions with SHELXE.
@nl
P2860
P1476
Extending molecular-replacement solutions with SHELXE.
@en
P2093
George M Sheldrick
P2860
P304
P356
10.1107/S0907444913027534
P50
P577
2013-10-18T00:00:00Z