Enhancing ubiquitin crystallization through surface-entropy reduction.

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Systematic analysis of residual density suggests that a major limitation in well-refined X-ray structures of proteins is the omission of ordered solvent.New crystal form of human ubiquitin in the presence of magnesium.

P2860

Q38937897-D72FBBC6-0939-49D6-B4B3-159592BE55B5 Q54867174-58C9DCA1-68DF-4DC5-A920-287C6D80F58C

P2860

Enhancing ubiquitin crystallization through surface-entropy reduction.

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http://www.wikidata.org/entity/Q42242652

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2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

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2014年論文

@zh-tw

2014年论文

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2014年论文

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2014年论文

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name

Enhancing ubiquitin crystallization through surface-entropy reduction.

@en

Enhancing ubiquitin crystallization through surface-entropy reduction.

@nl

type

Item

label

Enhancing ubiquitin crystallization through surface-entropy reduction.

@en

Enhancing ubiquitin crystallization through surface-entropy reduction.

@nl

prefLabel

Enhancing ubiquitin crystallization through surface-entropy reduction.

@en

Enhancing ubiquitin crystallization through surface-entropy reduction.

@nl

P1476

Enhancing ubiquitin crystallization through surface-entropy reduction.

@en

P2093

John T Schmidt

http://www.w3.org/2001/XMLSchema#string

Patrick J Loll

http://www.w3.org/2001/XMLSchema#string

Peining Xu

http://www.w3.org/2001/XMLSchema#string

Scott L Melideo

http://www.w3.org/2001/XMLSchema#string

P2860

Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne

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Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI

Protein crystallization by surface entropy reduction: optimization of the SER strategy

Crystal structures of Lys-63-linked tri- and di-ubiquitin reveal a highly extended chain architecture

K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody

Structure of the complex between teicoplanin and a bacterial cell-wall peptide: use of a carrier-protein approach

A Carrier Protein Strategy Yields the Structure of Dalbavancin

Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes

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1434-1442

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scholarly article

P356

10.1107/S2053230X14019244

http://www.w3.org/2001/XMLSchema#string

P433

Pt 10

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2014-09-25T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

25286958

http://www.w3.org/2001/XMLSchema#string

P932

4188098

http://www.w3.org/2001/XMLSchema#string

Enhancing ubiquitin crystallization through surface-entropy reduction.

about

P2860

P2860

Enhancing ubiquitin crystallization through surface-entropy reduction.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932