ARP/wARP and molecular replacement: the next generation. - Wikidata - awgldk - TriplyDB

ARP/wARP and molecular replacement: the next generation.

ARP/wARP and molecular replacement: the next generation.

http://www.wikidata.org/entity/Q38606646

about

Structure of the head of the Bartonella adhesin BadA X-ray crystal structure of the streptococcal specific phage lysin PlyC.Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation Structure and Function of Colicin S4, a Colicin with a Duplicated Receptor-binding Domain Unusual Armadillo Fold in the Human General Vesicular Transport Factor p115 Structure of granzyme C reveals an unusual mechanism of protease autoinhibition Active-Site Gating Regulates Substrate Selectivity in a Chymotrypsin-Like Serine Protease Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIÎ² binding protein 1 N-Myristoyltransferase from Leishmania donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases.Type-zero copper proteins Structural Basis of Fatty Acid Substrate Binding to Cyclooxygenase-2 Crystal structure and ligand binding of the MID domain of a eukaryotic Argonaute protein Central Region of Talin Has a Unique Fold That Binds Vinculin and Actin Structure of a fibronectin type III-like module fromClostridium thermocellum Evolution of I-SceI Homing Endonucleases with Increased DNA Recognition Site Specificity The crystal structures of theSalmonellatype III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholate Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2 Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control Structural basis of cooperative DNA recognition by the plasmid conjugation factor, TraM Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana Structure of the signal transduction protein TRAP (target of RNAIII-activating protein)Insights into the inhibition of the p90 ribosomal S6 kinase (RSK) by the flavonol glycoside SL0101 from the 1.5 Å crystal structure of the N-terminal domain of RSK2 with bound inhibitor.Structure ofAeropyrum pernixfibrillarin in complex with natively boundS-adenosyl-L-methionine at 1.7 Å resolution Structure of a tetrameric galectin fromCinachyrellasp. (ball sponge)Structure of the prolyl-tRNA synthetase from the eukaryotic pathogenGiardia lamblia The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization Single Cystathionine -Synthase Domain-Containing Proteins Modulate Development by Regulating the Thioredoxin System in Arabidopsis Evolution to carbapenem-hydrolyzing activity in noncarbapenemase class D -lactamase OXA-10 by rational protein design Identification of quercitrin as an inhibitor of the p90 S6 ribosomal kinase (RSK): structure of its complex with the N-terminal domain of RSK2 at 1.8 Å resolution The structure of the Bach2 POZ-domain dimer reveals an intersubunit disulfide bond Studies on an ( S )-2-Amino-3-(3-hydroxy-5-methyl-4-isoxazolyl)propionic Acid (AMPA) Receptor Antagonist IKM-159: Asymmetric Synthesis, Neuroactivity, and Structural Characterization The TP0796 Lipoprotein of Treponema pallidum Is a Bimetal-dependent FAD Pyrophosphatase with a Potential Role in Flavin Homeostasis Structure ofVibrio choleraeribosome hibernation promoting factor Structure and function of the Clostridium thermocellum cellobiohydrolase A X1-module repeat: enhancement through stabilization of the CbhA complex The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4 Structural Insights into Recognition of MDC1 by TopBP1 in DNA Replication Checkpoint Control Crystal Structure of the Mobile Metallo- -Lactamase AIM-1 from Pseudomonas aeruginosa: Insights into Antibiotic Binding and the Role of Gln157 Structure and properties of the esterase from non-LTR retrotransposons suggest a role for lipids in retrotransposition

P2860

Q21131595-DEFB5B23-6544-4C28-B589-F60484F12F45 Q24623471-6CBE65A4-80B3-4EA1-81CF-E8CF436A423B Q24633548-26497FAF-7894-4078-AAF9-8B800A32E45C Q27653060-8396366C-BF96-4BFC-A5A2-712EA0011D03 Q27653959-8747E236-04F4-49F4-B97E-D4875A77F740 Q27654213-DB4B0D7D-C5AC-4927-B43E-EC65B2FB79B9 Q27655228-26ADC3E1-3BAA-48A3-AFA2-6CCFEDC12F80 Q27658324-16B7A368-6ACE-4514-8CC3-4024DBA848AE Q27658775-A2EC1F03-9F5C-4E14-B22A-74AB2826380D Q27659580-1B9E121E-3A2F-44E0-9BC8-E132F10F75DA Q27660299-0218C87A-B902-4AA9-BC02-B2D376B4B4B9 Q27661560-3D2460CC-803C-482D-994A-51A0D124DBA2 Q27662170-A021D4F5-E53C-4E4B-97A1-1DC7D308910C Q27663253-6F26D56A-E823-4F1B-B66E-7F00BC9363A1 Q27663908-8D7C8173-73DF-47E6-B4E6-C64EA2AB0D2E Q27665420-F1EF192B-72BB-419D-A714-1B8E8CA9D8C5 Q27665429-1B3EA18B-998B-476D-BAA1-462562C66E78 Q27665857-9708290A-5233-442D-A22C-D701FAEAD2FF Q27666163-0E782261-1BE4-4A64-A00C-401C79595265 Q27667824-5DAC8863-F405-4BC3-858B-97AC4B4DFE3C Q27667838-B7A2F80C-0928-4846-AADF-9A86B1A21CA4 Q27670581-BAC0CE50-6856-4C0E-8ADF-56F605B1A075 Q27670966-C0FBAA20-A6C8-4853-95D4-57C9075636D4 Q27671203-8A09A36D-8771-41B1-8B83-E16EDE4BC2CC Q27671912-D34CEA98-4A57-460C-8F61-76F3E5AD41A2 Q27671923-EC3BC329-1590-41CF-BB13-1040D26DB55E Q27675142-22DD08FE-2390-48EB-8D13-2BE664F3E703 Q27675186-6B6B210C-ECD2-4CEC-9D51-3FC02CA72EEB Q27675331-2C87D9E8-0AA1-4BE5-9720-163A22D98ADC Q27676158-B8A0AC71-38E4-43FF-9A1C-C0F18876EE95 Q27676372-0B5E5F39-8ACD-48D7-9368-E78421A61CA0 Q27676563-027B7DF8-147F-4756-9914-1360E7928DAC Q27676647-8AE8F0DA-C3FA-4807-A20F-EB20CBBC2F00 Q27676970-56BB12AD-AF04-4137-B628-53F85F383F36 Q27677377-9C792B8E-DCAD-44F4-9CD0-93EDD7CC30F1 Q27677938-2C98B974-B1CE-4609-83F3-95510B4AA818 Q27678981-9AAF13E4-20F1-42A9-AF19-5BEE7F89FEB5 Q27679213-3C24422D-5842-42BE-905D-56CED00FAE9D Q27679496-F9600204-3340-4CC9-B94D-005E64CC8CF3 Q27679864-07AF3A5A-E0BF-4537-8BBD-B1C0B3CA8EF6

P2860

ARP/wARP and molecular replacement: the next generation.

http://www.wikidata.org/entity/Q38606646

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

ARP/wARP and molecular replacement: the next generation.

@en

type

label

ARP/wARP and molecular replacement: the next generation.

@en

prefLabel

ARP/wARP and molecular replacement: the next generation.

@en

P1433

Q38606646-8563819D-2B87-4631-84E9-E3C645DD49B6

P1476

Q38606646-F1F8F9E4-6486-4C51-B5AE-7BD93D89F46E

P2093

Q38606646-05CF6F99-050B-4B45-8BBA-10EF56D71956

Q38606646-8B06A475-E84B-4290-A64F-40CE07EF08B7

Q38606646-AB0C0BFE-3A4B-418F-8D5B-0D849BE17995

Q38606646-B39DA7E7-8D44-490E-9B78-903B8CD0DFA7

Q38606646-B6FA8854-4DEB-4045-95F3-80F64A6F3050

Q38606646-DFB3442F-F2CB-4301-86A3-CEE3D17F433E

Q38606646-F10F1220-A2C2-41AA-852F-C918E45D6F59

P2860

Q38606646-03BF4BFC-AB07-4D16-A72F-4C5602C67C85

Q38606646-2623F4BF-4D34-4960-8B37-B239E78C4E11

Q38606646-272813AA-BB45-4911-8A33-BEF6CEEEA444

Q38606646-2975CF97-E09E-4912-A9A3-FB1436AC88DB

Q38606646-2C4AEDC3-0399-44B5-8C5E-7E5568081B38

Q38606646-3E11E3C6-AC31-484C-ABA4-D31FC9ECFACE

Q38606646-412EB589-F164-4B0B-A64F-476116DDD71D

Q38606646-45E10819-CDE8-4954-852B-62D99461A33D

Q38606646-56C6B881-5B3F-4F37-90BC-0A97742483AD

Q38606646-69B69976-C2E5-4ECB-9F28-D52918EF314B

P304

Q38606646-B3FBF5EE-1FD3-4126-90C4-B893BA868C4E

P31

Q38606646-05050F77-E012-45CB-816E-0744E127D43D

P356

Q38606646-68347756-F71E-4345-A63C-C090EAD25E43

P433

Q38606646-D312361C-8031-4FD5-BF57-EB4DED08FAC1

P478

Q38606646-675B49B0-6F57-4BB7-AFA5-9BCD7A736767

P50

Q38606646-25148DB9-BD17-45AE-BECE-E675C2454587

Q38606646-4652A459-7F62-4D0F-BF67-6497EABAF5A2

Q38606646-B4673A52-F5A6-489B-AD2F-046525E05B32

P577

Q38606646-FD435287-0CB4-4B71-9655-77A71919A0C1

P698

Q38606646-9C64CD42-AE28-4C51-A488-429852FE8061

P932

Q38606646-3C4063CE-6D67-4530-98AC-A621CA8D9E16

P356

S0907444907047580

P1433

Acta Crystallographica Section D: Biological Crystallography

P1476

ARP/wARP and molecular replacement: the next generation.

@en

P2093

Alexei Vagin

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

Fei Long

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

Garib N Murshudov

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

Joyce Lebbink

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

Marouane Ben Jelloul

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

Puck Knipscheer

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

Serge X Cohen

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

P2860

Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation

SOLVE and RESOLVE: automated structure solution, density modification and model building

Coot: model-building tools for molecular graphics

Automated protein model building combined with iterative structure refinement

BALBES: a molecular-replacement pipeline

ARP/wARP and molecular replacement

Automated refinement of protein models

Phasercrystallographic software

The Buccaneer software for automated model building. 1. Tracing protein chains

Refinement of macromolecular structures by the maximum-likelihood method

P304

49-60

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

P31

scholarly article

P356

10.1107/S0907444907047580

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

P433

Pt 1

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

P478

64

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

P50

Anastassis Perrakis

P577

2007-12-05T00:00:00Z

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

P698

18094467

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

P932

2394809

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