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  1 / 8219 MEDLINE  
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[PMID]:29184919
[Au] Autor:Luo Z; Friscic T; Khaliullin RZ
[Ad] Endereço:Department of Chemistry, McGill University, 801 Sherbrooke St. West, Montreal, QC H3A 0B8, Canada. rustam@khaliullin.com.
[Ti] Título:Why pregnenolone and progesterone, two structurally similar steroids, exhibit remarkably different cocrystallization with aromatic molecules.
[So] Source:Phys Chem Chem Phys;20(2):898-904, 2018 Jan 03.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Selective binding of steroid molecules is of paramount importance for designing drugs that can target the biological pathways of only individual steroids. From this perspective, it is remarkable that progesterone (PRO) and pregnenolone (PRE), two structurally similar steroids, demonstrate a dramatically different propensity to interact with aromatic molecules. It has been recently reported that, in solid-state cocrystallization, PRO forms cocrystals with a wide variety of aromatic systems whereas PRE cocrystallizes only with a few. In this work, a simple yet effective computational procedure was developed to explain the fundamental origins of this surprising phenomenon. This procedure enables a direct comparison of the strength of intermolecular binding in the structurally similar cocrystals of PRO and PRE by generating experimentally inaccessible meta-stable cocrystals of PRE that closely resemble those observed for PRO. Direct comparative analysis shows that interactions between the α-face of the steroid and the π-electrons of aromatic molecules, the focus of previous studies, are not sufficiently different to explain the cocrystallization behavior of PRO and PRE. Instead, the observed difference is attributed to the different stabilities of the cocrystals relative to their pure components: organic and steroid crystals. It is calculated that the cocrystallization process is thermodynamically favorable in the case of PRO and unfavorable in the case of PRE. Furthermore, strong hydrogen bonds in the pure PRE crystal appear to be the major factor that makes the cocrystallization of PRE energetically unfavorable for a wide range of aromatic molecules. The fundamental analysis performed in this work has important practical implications for designing new steroid-containing crystals, selective biomolecular steroid receptors, and steroid-specific drugs. It suggests that a strategy for the selective binding of steroids should focus primarily on tuning the strength of hydrogen bonding.
[Mh] Termos MeSH primário: Ligações de Hidrogênio
Pregnenolona/química
Progesterona/química
[Mh] Termos MeSH secundário: Cristalização
Cristalografia
Desenho de Drogas
Elétrons
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
4G7DS2Q64Y (Progesterone); 73R90F7MQ8 (Pregnenolone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp06828j


  2 / 8219 MEDLINE  
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[PMID]:29205914
[Au] Autor:Wlodawer A
[Ad] Endereço:Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD, USA.
[Ti] Título:Online tools for enhancing presentation, understanding, and retention of 3D structural data.
[So] Source:FEBS J;284(23):3974-3976, 2017 Dec.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dr Alexander Wlodawer, an Editor for The FEBS Journal, provides an overview of three useful resources for structural biologists: Protopedia, Molstack and the Integrated Resource for Reproducibility in Macromolecular Crystallography (IRRMC).
[Mh] Termos MeSH primário: Biologia Computacional/métodos
Internet
Sistemas On-Line
Conformação Proteica
[Mh] Termos MeSH secundário: Cristalografia
Seres Humanos
Modelos Moleculares
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:EDITORIAL
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14316


  3 / 8219 MEDLINE  
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[PMID]:29036200
[Au] Autor:Covaceuszach S; Bozzi M; Bigotti MG; Sciandra F; Konarev PV; Brancaccio A; Cassetta A
[Ad] Endereço:Istituto di Cristallografia-CNR, Trieste Outstation, Trieste, Italy.
[Ti] Título:The effect of the pathological V72I, D109N and T190M missense mutations on the molecular structure of α-dystroglycan.
[So] Source:PLoS One;12(10):e0186110, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dystroglycan (DG) is a highly glycosylated protein complex that links the cytoskeleton with the extracellular matrix, mediating fundamental physiological functions such as mechanical stability of tissues, matrix organization and cell polarity. A crucial role in the glycosylation of the DG α subunit is played by its own N-terminal region that is required by the glycosyltransferase LARGE. Alteration in this O-glycosylation deeply impairs the high affinity binding to other extracellular matrix proteins such as laminins. Recently, three missense mutations in the gene encoding DG, mapped in the α-DG N-terminal region, were found to be responsible for hypoglycosylated states, causing congenital diseases of different severity referred as primary dystroglycanopaties.To gain insight on the molecular basis of these disorders, we investigated the crystallographic and solution structures of these pathological point mutants, namely V72I, D109N and T190M. Small Angle X-ray Scattering analysis reveals that these mutations affect the structures in solution, altering the distribution between compact and more elongated conformations. These results, supported by biochemical and biophysical assays, point to an altered structural flexibility of the mutant α-DG N-terminal region that may have repercussions on its interaction with LARGE and/or other DG-modifying enzymes, eventually reducing their catalytic efficiency.
[Mh] Termos MeSH primário: Distroglicanas/química
Distroglicanas/genética
Mutação de Sentido Incorreto
[Mh] Termos MeSH secundário: Animais
Cristalografia
Distroglicanas/metabolismo
Estabilidade Enzimática
Fluorometria
Camundongos
Modelos Moleculares
Mutagênese Sítio-Dirigida
Desnaturação Proteica
Espalhamento a Baixo Ângulo
Soluções
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Solutions); 146888-27-9 (Dystroglycans)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186110


  4 / 8219 MEDLINE  
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[PMID]:28994413
[Au] Autor:Papp G; Felisaz F; Sorez C; Lopez-Marrero M; Janocha R; Manjasetty B; Gobbo A; Belrhali H; Bowler MW; Cipriani F
[Ad] Endereço:European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, CS 90181, 38042 Grenoble, France.
[Ti] Título:FlexED8: the first member of a fast and flexible sample-changer family for macromolecular crystallography.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 10):841-851, 2017 Oct 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Automated sample changers are now standard equipment for modern macromolecular crystallography synchrotron beamlines. Nevertheless, most are only compatible with a single type of sample holder and puck. Recent work aimed at reducing sample-handling efforts and crystal-alignment times at beamlines has resulted in a new generation of compact and precise sample holders for cryocrystallography: miniSPINE and NewPin [see the companion paper by Papp et al. (2017, Acta Cryst., D73, 829-840)]. With full data collection now possible within seconds at most advanced beamlines, and future fourth-generation synchrotron sources promising to extract data in a few tens of milliseconds, the time taken to mount and centre a sample is rate-limiting. In this context, a versatile and fast sample changer, FlexED8, has been developed that is compatible with the highly successful SPINE sample holder and with the miniSPINE and NewPin sample holders. Based on a six-axis industrial robot, FlexED8 is equipped with a tool changer and includes a novel open sample-storage dewar with a built-in ice-filtering system. With seven versatile puck slots, it can hold up to 112 SPINE sample holders in uni-pucks, or 252 miniSPINE or NewPin sample holders, with 36 samples per puck. Additionally, a double gripper, compatible with the SPINE sample holders and uni-pucks, allows a reduction in the sample-exchange time from 40 s, the typical time with a standard single gripper, to less than 5 s. Computer vision-based sample-transfer monitoring, sophisticated error handling and automatic error-recovery procedures ensure high reliability. The FlexED8 sample changer has been successfully tested under real conditions on a beamline.
[Mh] Termos MeSH primário: Cristalografia/instrumentação
[Mh] Termos MeSH secundário: Cristalografia/economia
Desenho de Equipamento
Proteínas/química
Robótica/economia
Robótica/instrumentação
Manejo de Espécimes
Temperatura Ambiente
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317013596


  5 / 8219 MEDLINE  
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[PMID]:28994412
[Au] Autor:Papp G; Rossi C; Janocha R; Sorez C; Lopez-Marrero M; Astruc A; McCarthy A; Belrhali H; Bowler MW; Cipriani F
[Ad] Endereço:European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, CS 90181, 38042 Grenoble, France.
[Ti] Título:Towards a compact and precise sample holder for macromolecular crystallography.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 10):829-840, 2017 Oct 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most of the sample holders currently used in macromolecular crystallography offer limited storage density and poor initial crystal-positioning precision upon mounting on a goniometer. This has now become a limiting factor at high-throughput beamlines, where data collection can be performed in a matter of seconds. Furthermore, this lack of precision limits the potential benefits emerging from automated harvesting systems that could provide crystal-position information which would further enhance alignment at beamlines. This situation provided the motivation for the development of a compact and precise sample holder with corresponding pucks, handling tools and robotic transfer protocols. The development process included four main phases: design, prototype manufacture, testing with a robotic sample changer and validation under real conditions on a beamline. Two sample-holder designs are proposed: NewPin and miniSPINE. They share the same robot gripper and allow the storage of 36 sample holders in uni-puck footprint-style pucks, which represents 252 samples in a dry-shipping dewar commonly used in the field. The pucks are identified with human- and machine-readable codes, as well as with radio-frequency identification (RFID) tags. NewPin offers a crystal-repositioning precision of up to 10 µm but requires a specific goniometer socket. The storage density could reach 64 samples using a special puck designed for fully robotic handling. miniSPINE is less precise but uses a goniometer mount compatible with the current SPINE standard. miniSPINE is proposed for the first implementation of the new standard, since it is easier to integrate at beamlines. An upgraded version of the SPINE sample holder with a corresponding puck named SPINEplus is also proposed in order to offer a homogenous and interoperable system. The project involved several European synchrotrons and industrial companies in the fields of consumables and sample-changer robotics. Manual handling of miniSPINE was tested at different institutes using evaluation kits, and pilot beamlines are being equipped with compatible robotics for large-scale evaluation. A companion paper describes a new sample changer FlexED8 (Papp et al., 2017, Acta Cryst., D73, 841-851).
[Mh] Termos MeSH primário: Cristalografia/instrumentação
[Mh] Termos MeSH secundário: Desenho de Equipamento
Robótica/instrumentação
Tamanho da Amostra
Síncrotrons
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317013742


  6 / 8219 MEDLINE  
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[PMID]:28864445
[Au] Autor:Cuthbert BJ; Ross W; Rohlfing AE; Dove SL; Gourse RL; Brennan RG; Schumacher MA
[Ad] Endereço:Department of Biochemistry, Duke University School of Medicine, Durham, North Carolina 27710, USA.
[Ti] Título:Dissection of the molecular circuitry controlling virulence in .
[So] Source:Genes Dev;31(15):1549-1560, 2017 Aug 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:the etiological agent of tularemia, is one of the most infectious bacteria known. Because of its extreme pathogenicity, is classified as a category A bioweapon by the US government. virulence stems from genes encoded on the pathogenicity island (FPI). An unusual set of regulators-the heteromeric macrophage growth locus protein A (MglA)-stringent starvation protein A (SspA) complex and the DNA-binding protein pathogenicity island gene regulator (PigR)-activates FPI transcription and thus is essential for virulence. Intriguingly, the second messenger, guanosine-tetraphosphate (ppGpp), which is produced during infection, is also involved in coordinating virulence; however, its role has been unclear. Here we identify MglA-SspA as a novel ppGpp-binding complex and describe structures of apo- and ppGpp-bound MglA-SspA. We demonstrate that MglA-SspA, which binds RNA polymerase (RNAP), also interacts with the C-terminal domain of PigR, thus anchoring the (MglA-SspA)-RNAP complex to the FPI promoter. Furthermore, we show that MglA-SspA must be bound to ppGpp to mediate high-affinity interactions with PigR. Thus, these studies unveil a novel pathway different from those described previously for regulation of transcription by ppGpp. The data also indicate that pathogenesis is controlled by a highly interconnected molecular circuitry in which the virulence machinery directly senses infection via a small molecule stress signal.
[Mh] Termos MeSH primário: Adesinas Bacterianas/metabolismo
Proteínas de Ligação a DNA/metabolismo
Francisella tularensis/patogenicidade
Ilhas Genômicas/genética
Guanosina Tetrafosfato/metabolismo
Tularemia/microbiologia
[Mh] Termos MeSH secundário: Adesinas Bacterianas/química
Adesinas Bacterianas/genética
Bioterrorismo/prevenção & controle
Células Cultivadas
Cristalografia
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/genética
RNA Polimerases Dirigidas por DNA/metabolismo
Regulação Bacteriana da Expressão Gênica
Guanosina Tetrafosfato/genética
Seres Humanos
Macrófagos/metabolismo
Conformação Proteica
Transcrição Genética
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (DNA-Binding Proteins); 0 (SspA protein, bacteria); 33503-72-9 (Guanosine Tetraphosphate); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1101/gad.303701.117


  7 / 8219 MEDLINE  
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[PMID]:28777085
[Au] Autor:Naitow H; Matsuura Y; Tono K; Joti Y; Kameshima T; Hatsui T; Yabashi M; Tanaka R; Tanaka T; Sugahara M; Kobayashi J; Nango E; Iwata S; Kunishima N
[Ad] Endereço:Bio-Specimen Platform Group, RIKEN SPring-8 Center, Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
[Ti] Título:Protein-ligand complex structure from serial femtosecond crystallography using soaked thermolysin microcrystals and comparison with structures from synchrotron radiation.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 8):702-709, 2017 Aug 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serial femtosecond crystallography (SFX) with an X-ray free-electron laser is used for the structural determination of proteins from a large number of microcrystals at room temperature. To examine the feasibility of pharmaceutical applications of SFX, a ligand-soaking experiment using thermolysin microcrystals has been performed using SFX. The results were compared with those from a conventional experiment with synchrotron radiation (SR) at 100 K. A protein-ligand complex structure was successfully obtained from an SFX experiment using microcrystals soaked with a small-molecule ligand; both oil-based and water-based crystal carriers gave essentially the same results. In a comparison of the SFX and SR structures, clear differences were observed in the unit-cell parameters, in the alternate conformation of side chains, in the degree of water coordination and in the ligand-binding mode.
[Mh] Termos MeSH primário: Cristalografia/métodos
Geobacillus stearothermophilus/química
Geobacillus stearothermophilus/enzimologia
Termolisina/química
[Mh] Termos MeSH secundário: Cristalização/métodos
Cristalografia por Raios X/métodos
Desenho de Drogas
Geobacillus stearothermophilus/metabolismo
Ligantes
Modelos Moleculares
Conformação Proteica
Síncrotrons
Termolisina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); EC 3.4.24.27 (Thermolysin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317008919


  8 / 8219 MEDLINE  
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[PMID]:28760339
[Au] Autor:Koyama M; Matsuura Y
[Ad] Endereço:Division of Biological Science, Graduate School of Science, Nagoya University, Japan.
[Ti] Título:Crystal structure of importin-α3 bound to the nuclear localization signal of Ran-binding protein 3.
[So] Source:Biochem Biophys Res Commun;491(3):609-613, 2017 Sep 23.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ran-binding protein 3 (RanBP3) is a primarily nuclear Ran-binding protein that functions as an accessory factor in the Ran GTPase system. RanBP3 associates with Ran-specific nucleotide exchange factor RCC1 and enhances its catalytic activity towards Ran. RanBP3 also promotes CRM1-mediated nuclear export as well as CRM1-independent nuclear export of ß-catenin, Smad2, and Smad3. Nuclear import of RanBP3 is dependent on the nuclear import adaptor protein importin-α and, RanBP3 is imported more efficiently by importin-α3 than by other members of the importin-α family. Protein kinase signaling pathways control nucleocytoplasmic transport through phosphorylation of RanBP3 at Ser58, immediately C-terminal to the nuclear localization signal (NLS) in the N-terminal region of RanBP3. Here we report the crystal structure of human importin-α3 bound to an N-terminal fragment of human RanBP3 containing the NLS sequence that is necessary and sufficient for nuclear import. The structure reveals that RanBP3 binds to importin-α3 residues that are strictly conserved in all seven isoforms of human importin-α at the major NLS-binding site, indicating that the region of importin-α outside the NLS-binding site, possibly the autoinhibotory importin-ß1-binding domain, may be the key determinant for the preferential binding of RanBP3 to importin-α3. Computational docking simulation indicates that phosphorylation of RanBP3 at Ser58 could potentially stabilize the association of RanBP3 with importin-α through interactions between the phosphate moiety of phospho-Ser58 of RanBP3 and a cluster of basic residues (Arg96 and Lys97 in importin-α3) on armadillo repeat 1 of importin-α.
[Mh] Termos MeSH primário: Proteínas de Drosophila/química
Proteínas de Drosophila/ultraestrutura
Modelos Químicos
Simulação de Acoplamento Molecular
Sinais de Localização Nuclear/química
Proteínas Nucleares/química
Proteínas Nucleares/ultraestrutura
Proteínas de Transporte Nucleocitoplasmático/química
Proteínas de Transporte Nucleocitoplasmático/ultraestrutura
alfa Carioferinas/química
alfa Carioferinas/ultraestrutura
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalografia
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Kap-alpha3 protein, Drosophila); 0 (Nuclear Localization Signals); 0 (Nuclear Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RANBP3 protein, human); 0 (alpha Karyopherins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


  9 / 8219 MEDLINE  
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[PMID]:28758290
[Au] Autor:Wen Y; Ouyang Z; Devreese B; He W; Shao Y; Lu W; Zheng F
[Ad] Endereço:Center for Translational Medicine, The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an, China.
[Ti] Título:Crystal structure of master biofilm regulator CsgD regulatory domain reveals an atypical receiver domain.
[So] Source:Protein Sci;26(10):2073-2082, 2017 Oct.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The master regulator CsgD switches planktonic growth to biofilm formation by activating synthesis of curli fimbriae and cellulose in Enterobacteriaceae. CsgD was classified to be the LuxR response regulatory family, while its cognate sensor histidine kinase has not been identified yet. CsgD consists of a C-terminal DNA binding domain and an N-terminal regulatory domain that provokes the upstream signal transduction to further modulate its function. We provide the crystal structure of Salmonella Typhimurium CsgD regulatory domain, which reveals an atypical ß5α5 response regulatory receiver domain folding with the α2 helix representing as a disorder loop compared to the LuxR/FixJ canonical response regulator, and the structure indicated a noteworthy α5 helix similar to the non-canonical master regulator VpsT receiver domain α6. CsgD regulatory domain assembles with two dimerization interfaces mainly through α1 and α5, which has shown similarity to the c-di-GMP independent and stabilized dimerization interface of VpsT from Vibrio cholerae respectively. The potential phosphorylation site D59 is directly involved in the interaction of interfaces I and mutagenesis studies indicated that both dimerization interfaces could be crucial for CsgD activity. The structure reveals important molecular details for the dimerization assembly of CsgD and will shed new insight into its regulation mechanism.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Transativadores/química
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Biofilmes
Cristalografia
Fosforilação
Domínios Proteicos
Salmonella typhimurium/química
Salmonella typhimurium/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Trans-Activators)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3245


  10 / 8219 MEDLINE  
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[PMID]:28733116
[Au] Autor:Johansson LC; Stauch B; Ishchenko A; Cherezov V
[Ad] Endereço:Department of Chemistry, Bridge Institute, University of Southern California, Los Angeles, CA 90089-3303, USA.
[Ti] Título:A Bright Future for Serial Femtosecond Crystallography with XFELs.
[So] Source:Trends Biochem Sci;42(9):749-762, 2017 Sep.
[Is] ISSN:0968-0004
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular structural biology due to the unique combination of spatial coherence, extreme peak brilliance, and short duration of X-ray pulses. A recently emerged serial femtosecond (fs) crystallography (SFX) approach using XFEL radiation overcomes some of the biggest hurdles of traditional crystallography related to radiation damage through the diffraction-before-destruction principle. Intense fs XFEL pulses enable high-resolution room-temperature structure determination of difficult-to-crystallize biological macromolecules, while simultaneously opening a new era of time-resolved structural studies. Here, we review the latest developments in instrumentation, sample delivery, data analysis, crystallization methods, and applications of SFX to important biological questions, and conclude with brief insights into the bright future of structural biology using XFELs.
[Mh] Termos MeSH primário: Cristalografia/métodos
Elétrons
Lasers
[Mh] Termos MeSH secundário: Substâncias Macromoleculares/química
Fatores de Tempo
Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Macromolecular Substances)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170723
[St] Status:MEDLINE



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde