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The collection includes articles from PSI research groups and the broader community

January 2011

  • High-resolution structure of the nitrile reductase QueF combined with molecular simulations provide insight into enzyme mechanism

    Kim Y., Zhou M., Moy S., Morales J., Cunningham M. et al.

    J Mol Biol 404, 127 - 137 (2010)

    [doi: http://dx.doi.org/10.1016/j.jmb.2010.09.042]

  • The JCSG high-throughput structural biology pipeline

    Elsliger M., Deacon A., Godzik A., Lesley S., Wooley J. et al.

    Acta Cryst F 66, 1137 - 1142 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110038212]

  • TOPSAN: use of a collaborative environment for annotating, analyzing and disseminating data on JCSG and PSI structures

    Krishna S., Weekes D., Bakolitsa C., Elsliger M., Wilson I. et al.

    Acta Cryst F 66, 1143 - 1147 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110035736]

  • DUFs: families in search of function

    Bateman A., Coggill P. and Finn R.

    Acta Cryst F 66, 1148 - 1152 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110001685]

  • Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism

    Chiu H., Bakolitsa C., Skerra A., Lomize A., Carlton D. et al.

    Acta Cryst F 66, 1153 - 1159 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109037749]

  • The structure of SSO2064, the first representative of Pfam family PF01796, reveals a novel two-domain zinc-ribbon OB-fold architecture with a potential acyl-CoA-binding role

    Krishna S., Aravind L., Bakolitsa C., Caruthers J., Carlton D. et al.

    Acta Cryst F 66, 1160 - 1166 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110002514]

  • Structure of the first representative of Pfam family PF04016 (DUF364) reveals enolase and Rossmann-like folds that combine to form a unique active site with a possible role in heavy-metal chelation

    Miller M., Aravind L., Bakolitsa C., Rife C., Carlton D. et al.

    Acta Cryst F 66, 1167 - 1173 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110007517]

  • The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation

    Das D., Grishin N., Kumar A., Carlton D., Bakolitsa C. et al.

    Acta Cryst F 66, 1174 - 1181 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109022672]

  • Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism

    Bakolitsa C., Kumar A., Jin K., McMullan D., Krishna S. et al.

    Acta Cryst F 66, 1182 - 1189 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109050647]

  • Structural classification of proteins and structural genomics: new insights into protein folding and evolution

    Andreeva A. and Murzin A.

    Acta Cryst F 66, 1190 - 1197 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110007177]

  • The structure of Jann_2411 (DUF1470) from Jannaschia sp. at 1.45 Å resolution reveals a new fold (the ABATE domain) and suggests its possible role as a transcription regulator

    Bakolitsa C., Bateman A., Jin K., McMullan D., Krishna S. et al.

    [doi: http://dx.doi.org/10.1107/S1744309109025196]

  • Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism

    Bakolitsa C., Kumar A., Carlton D., Miller M., Krishna S. et al.

    [doi: http://dx.doi.org/10.1107/S1744309109023689]

  • The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism

    Bakolitsa C., Kumar A., McMullan D., Krishna S., Miller M. et al.

    [doi: http://dx.doi.org/10.1107/S1744309109022684]

  • Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal transduction

    Han G., Bakolitsa C., Miller M., Kumar A., Carlton D. et al.

    [doi: http://dx.doi.org/10.1107/S1744309109050416]

  • New variants of known folds: do they bring new biology?

    Koonin E.

    Acta Cryst F 66, 1226 - 1229 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110013242]

  • Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution

    Xu Q., McMullan D., Jaroszewski L., Krishna S., Elsliger M. et al.

    Acta Cryst F 66, 1230 - 1236 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109022192]

  • Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15

    Han G., Elsliger M., Yeates T., Xu Q., Murzin A. et al.

    Acta Cryst F 66, 1237 - 1244 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110025534]

  • Open and closed conformations of two SpoIIAA-like proteins (YP_749275.1 and YP_001095227.1) provide insights into membrane association and ligand binding

    Kumar A., Lomize A., Jin K., Carlton D., Miller M. et al.

    Acta Cryst F 66, 1245 - 1253 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109042481]

  • The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold

    Das D., Kozbial P., Han G., Carlton D., Jaroszewski L. et al.

    Acta Cryst F 66, 1254 - 1260 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109018168]

  • Viewing the human microbiome through three-dimensional glasses: integsrating structural and functional studies to better define the properties of myriad carbohydrate-active enzymes

    Turnbaugh P., Henrissat B. and Gordon J.

    Acta Cryst F 66, 1261 - 1264 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110029088]

  • The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory function

    Das D., Finn R., Carlton D., Miller M., Abdubek P. et al.

    Acta Cryst F 66, 1265 - 1273 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109046788]

  • Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules

    Bakolitsa C., Xu Q., Rife C., Abdubek P., Astakhova T. et al.

    Acta Cryst F 66, 1274 - 1280 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110032999]

  • A conserved fold for fimbrial components revealed by the crystal structure of a putative fimbrial assembly protein (BT1062) from Bacteroides thetaiotaomicron at 2.2 Å resolution

    Xu Q., Abdubek P., Astakhova T., Axelrod H., Bakolitsa C. et al.

    Acta Cryst F 66, 1281 - 1286 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110006548]

  • Structure of Bacteroides thetaiotaomicron BT2081 at 2.05 Å resolution: the first structural representative of a new protein family that may play a role in carbohydrate metabolism

    Yeh A., Abdubek P., Astakhova T., Axelrod H., Bakolitsa C. et al.

    Acta Cryst F 66, 1287 - 1296 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110028228]

  • Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicron

    Xu Q., Abdubek P., Astakhova T., Axelrod H., Bakolitsa C. et al.

    Acta Cryst F 66, 1297 - 1305 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110023055]

  • Ligands in crystal structures that aid in functional characterization

    Speers A. and Cravatt B.

    Acta Cryst F 66, 1306 - 1308 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110035748]

  • Ligands in PSI structures

    Kumar A., Chiu H., Axelrod H., Morse A., Elsliger M. et al.

    Acta Cryst F 66, 1309 - 1316 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110008092]

  • The structure of Haemophilus influenzaeprephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes

    Chiu H., Abdubek P., Astakhova T., Axelrod H., Carlton D. et al.

    Acta Cryst F 66, 1317 - 1325 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110021688]

  • Structure of a tryptophanyl-tRNA synthetase containing an iron-sulfur cluster

    Han G., Yang X., McMullan D., Chong Y., Krishna S. et al.

    Acta Cryst F 66, 1326 - 1334 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110037619]

  • Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc finger

    Axelrod H., Das D., Abdubek P., Astakhova T., Bakolitsa C. et al.

    Acta Cryst F 66, 1335 - 1346 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110020166]

  • Conformational changes associated with the binding of zinc acetate at the putative active site of XcTcmJ, a cupin from Xanthomonas campestris pv. campestris

    Axelrod H., Kozbial P., McMullan D., Krishna S., Miller M. et al.

    Acta Cryst F 66, 1347 - 1353 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309109021988]

  • Structure of the γ-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala-γ-D-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases

    Xu Q., Abdubek P., Astakhova T., Axelrod H., Bakolitsa C. et al.

    Acta Cryst F 66, 1354 - 1364 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110021214]

  • NMR in a crystallography-based high-throughput protein structure-determination environment

    Wüthrich K.

    Acta Cryst F 66, 1365 - 1366 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110030320]

  • NMR structure of the protein NP_247299.1: comparison with the crystal structure

    Jaudzems K., Geralt M., Serrano P., Mohanty B., Horst R. et al.

    Acta Cryst F 66, 1367 - 1380 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110005890]

  • Comparison of NMR and crystal structures for the proteins TM1112 and TM1367

    Mohanty B., Serrano P., Pedrini B., Jaudzems K., Geralt M. et al.

    Acta Cryst F 66, 1381 - 1392 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110020956]

  • Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites

    Serrano P., Pedrini B., Geralt M., Jaudzems K., Mohanty B. et al.

    Acta Cryst F 66, 1393 - 1405 (2010)

    [doi: http://dx.doi.org/10.1107/S1744309110033658]

  • Maltose–neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins

    Chae P., Rasmussen S., Rana R., Gotfryd K., Chandra R. et al.

    Nature Methods 7, 1003 (2010)

    [doi: http://dx.doi.org/10.1038/nmeth.1526]

  • The RNA structurome: high-throughput probing

    Westhof E.

    Nature Methods 7, 965 - 967 (2010)

    [doi: http://dx.doi.org/10.1038/nmeth1210-965]

  • Following the fold

    Doerr A.

    Nature Methods 7, 950 (2010)

    [doi: http://dx.doi.org/10.1038/nmeth1210-950]

  • Crystal Structure of the Eukaryotic Ribosome

    Ben-Shem A., Jenner L., Yusupova G. and Yusupov M.

    Science 330, 1203 - 1209 (2010)

    [doi: http://dx.doi.org/10.1126/science.1194294]

  • Crystal Structures of RNase H2 in Complex with Nucleic Acid Reveal the Mechanism of RNA-DNA Junction Recognition and Cleavage

    Rychlik M., Chon H., Cerritelli S., Klimek P., Crouch R. et al.

    Molecular Cell 40, 658 - 670 (2010)

    [doi: http://dx.doi.org/10.1016/j.molcel.2010.11.001]

  • N. meningitidis 1681 is a member of the FinO family of RNA chaperones

    Chaulk S., Lu J., Tan K., Arthur D., Edwards R. et al.

    RNA biol 7, 112 - 119 (2010)

    [http://www.landesbioscience.com/journals/rnabiology/article/13688]

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