Protein crystallization by surface entropy reduction: optimization of the SER strategy - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27644579

about

High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering Structural genomics and drug discovery for infectious diseases The Crystal Structure of a Binary Complex of two Pseudopilins: EpsI and EpsJ from the Type 2 Secretion System of Vibrio vulnificus An unexpected outcome of surface engineering an integral membrane protein: improved crystallization of cytochromeba3fromThermus thermophilus Structural insight into bioremediation of triphenylmethane dyes by Citrobacter sp. triphenylmethane reductase Improvement of crystal quality by surface mutations of β-lactamase Toho-1 Crystallographic and Biochemical Analysis of the Ran-binding Zinc Finger Domain Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from Pseudomonas aeruginosa PAO1 Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.The structure of DinB from Geobacillus stearothermophilus: a representative of a unique four-helix-bundle superfamily.Structural determinants of tobacco vein mottling virus protease substrate specificity Structural features and chaperone activity of the NudC protein family.Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis Lysine N -Decarboxylation Switch and Activation of the -Lactam Sensor Domain of BlaR1 Protein of Methicillin-resistant Staphylococcus aureus Structures of the Human Poly (ADP-Ribose) Glycohydrolase Catalytic Domain Confirm Catalytic Mechanism and Explain Inhibition by ADP-HPD Derivatives Architecture of the Soluble Receptor Aer2 Indicates an In-Line Mechanism for PAS and HAMP Domain Signaling Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB Crystal Structures of Malonyl-Coenzyme A Decarboxylase Provide Insights into Its Catalytic Mechanism and Disease-Causing Mutations Computational design of a protein crystal Split green fluorescent protein as a modular binding partner for protein crystallization Effects of protein engineering and rational mutagenesis on crystal lattice of single chain antibody fragments Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism Crystal structure of the mouse interleukin-3 β-receptor: insights into interleukin-3 binding and receptor activation Protein stability: a crystallographer's perspective Statistical analysis of crystallization database links protein physico-chemical features with crystallization mechanisms The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.The role of flexibility and molecular shape in the crystallization of proteins by surface mutagenesis A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data.Crysalis: an integrated server for computational analysis and design of protein crystallization.A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.Cleavable C-terminal His-tag vectors for structure determination.Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity.High-throughput protein purification and quality assessment for crystallization.New surface contacts formed upon reductive lysine methylation: improving the probability of protein crystallization.Application of protein engineering to enhance crystallizability and improve crystal properties.It's all in the crystals…The role of entropy and polarity in intermolecular contacts in protein crystals Protein crystallization in drug design: towards a rational approach.

P2860

Q24658210-9D268758-1B43-422F-B347-493763BA8A43 Q27490495-2F198C14-3FCD-4489-9A98-0365508C8349 Q27649091-45DE9C1F-BECE-49E1-931F-0183D288DA70 Q27649347-5DF9C7FE-9A70-414F-A6B7-EB22A723CAA5 Q27652068-ED2AB67D-27B6-4E19-A48C-D4A1C9D2A6C6 Q27654548-5E970975-F234-43B2-AC1D-083AB7DCF848 Q27655809-E26E826F-A528-4FB3-85F4-3DE362FB7F3E Q27656884-0A66FDD4-6AB1-410B-8B67-7AB8D6E792EF Q27658101-F4F2FAC3-CC63-4CC5-A24F-7BFAE299BBB8 Q27658256-ADA832F1-415A-46CB-8587-EE860B4BE31F Q27660134-A55AECA5-BD12-468C-8ACF-CC4F0181EE8B Q27664649-C320AB88-2D83-4831-B6F9-754F5F7CF03B Q27667619-93687FAF-5658-44BD-9905-1FC962817330 Q27670484-3DFFA4A5-DD01-41CE-97A3-8C4BAA513C12 Q27670911-6FB79E12-13B9-4BED-891F-CA6CDDB287CF Q27675530-9E3943DA-A18F-4570-9693-493F9C1102AA Q27675636-87C56BFD-93F2-4CFF-8AC1-D55C8E1B4405 Q27675735-0311B0F7-792A-4A5F-B2E4-46828C7CA152 Q27678727-E19F6F18-718E-442F-AF24-E23170490349 Q27678758-471632B9-41A8-4055-8C90-38A9551D7C29 Q27680775-AAA04865-B359-46A5-B82F-802F11D36EDB Q27682066-EEA9E6AF-FE73-4806-97AA-BC9573B3C495 Q27682984-7C7F2046-41C2-4BD5-9C8B-944E6B3D474C Q27694791-39E01147-C53F-4ABE-9267-A270CB4FA979 Q28068775-EFCC027C-F181-4892-96A8-3D18C6213092 Q28540267-28A3A36C-7431-4CD1-B655-088B13189B7E Q30252224-1692EB44-0DF3-4290-910D-2C898E44263B Q30300834-C8AD942B-AB94-4A6D-8A62-E0FC3A04A21F Q30373301-54D8E28C-7608-4791-AC7C-257EEE4CE19C Q30373905-2375488A-FD3E-4D99-8DC5-32AADCE3C6A6 Q30384803-952D34F8-B6FD-483C-9402-CF580D36A789 Q30386218-1FE781E6-236C-4EC4-A9C3-72B2D96DE29C Q30386460-BF3018E6-0F27-427F-B4D0-1971493B7ED6 Q30405313-C16BE346-D10A-4DA0-8AB3-AEECCFB3BB02 Q30406950-16543B71-E72B-4B65-83D4-10B87E61EACC Q30431672-133C458F-647C-4447-8375-F76A19A595D3 Q30432379-33A20AF9-C3F4-4BBA-A65E-87F013259CCE Q30432744-427633A4-495B-42B9-A287-E2BC5EF9CEE3 Q30436185-A1F0B4F0-76FB-4D95-A87E-2F1B690ED37A Q30456527-18F75A5F-BBD6-4D6E-A242-FB3242E5BFB8

P2860

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

http://www.wikidata.org/entity/Q27644579

description

2007 nî lūn-bûn

@nan

2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

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

@ast

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

@en

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

@nl

type

label

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

@ast

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

@en

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

@nl

prefLabel

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

@ast

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

@en

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

@nl

P1433

Q27644579-52FB2A55-A164-4108-8E94-E9E78731C560

P1476

Q27644579-39F60222-51D1-4A75-A6CD-E4CA671F3F7F

P2093

Q27644579-1D9A74DA-6CD2-4210-84DC-20CB2FAB54CD

Q27644579-29DD3770-D913-419C-8A62-DDDDB6B54077

Q27644579-869260B9-93E6-4E50-A9B7-3C6EE5726355

Q27644579-990D54DD-C2B3-47F9-9965-6D4207C4F6FA

Q27644579-D9767144-6191-4FFB-8A08-802FCA7DEFF0

Q27644579-E2C4BF90-8A61-4FF1-9CC2-06B074560160

P304

Q27644579-D0C42265-9911-4F4B-8FC9-7157A3B06CEE

P31

Q27644579-DEB6BB9B-3E77-4C60-BD7B-27A6A76C0906

P356

Q27644579-8A86266A-9EF1-404B-9AAB-161037E00587

P433

Q27644579-926A8E99-C973-494B-BDFB-64D228352CB1

P478

Q27644579-2DF30C04-9C05-430E-B36A-D3070C73D51F

P50

Q27644579-8782D0AE-29B7-4226-974C-F9A8D236E983

P577

Q27644579-7724D1CE-D9D7-402B-A0EE-666563268FD2

P698

Q27644579-4422F964-6A39-4CE5-AF55-3CEFB4EB7E27

P356

S0907444907010931

P1433

Acta Crystallographica Section D: Biological Crystallography

P1476

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

@en

P2093

David R Cooper

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

Malgorzata Pinkowska

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

Malgorzata Sikorska

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

Michal Zawadzki

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

Tomasz Boczek

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

Zygmunt Derewenda

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

P304

636-645

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

P31

scholarly article

P356

10.1107/S0907444907010931

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

P433

Pt 5

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

P478

63

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

P50

Katarzyna Grelewska

P577

2007-04-21T00:00:00Z

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

P698

17452789

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