메뉴 건너뛰기




Volumn 22, Issue 9, 2014, Pages 1363-1371

Dramatic improvement of crystals of large RNAs by cation replacement and dehydration

Author keywords

[No Author keywords available]

Indexed keywords

CATION; COUNTERION; LITHIUM ION; MAGNESIUM ION; RNA; TRANSFER RNA; LITHIUM DERIVATIVE; LITHIUM SULFATE; MAGNESIUM; RIBOSWITCH; STRONTIUM; SULFATE;

EID: 84929317576     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.07.011     Document Type: Article
Times cited : (46)

References (45)
  • 3
    • 84863338217 scopus 로고    scopus 로고
    • YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops
    • N.J. Baird, J. Zhang, T. Hamma, and A.R. Ferré-D'Amaré YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops RNA 18 2012 759 770
    • (2012) RNA , vol.18 , pp. 759-770
    • Baird, N.J.1    Zhang, J.2    Hamma, T.3    Ferré-D'Amaré, A.R.4
  • 4
    • 4744359693 scopus 로고    scopus 로고
    • Turning protein crystallisation from an art into a science
    • N.E. Chayen Turning protein crystallisation from an art into a science Curr. Opin. Struct. Biol. 14 2004 577 583
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 577-583
    • Chayen, N.E.1
  • 5
    • 84881665613 scopus 로고    scopus 로고
    • Structural biology: RNA exerts self-control
    • B. Chetnani, and A. Mondragón Structural biology: RNA exerts self-control Nature 500 2013 279 280
    • (2013) Nature , vol.500 , pp. 279-280
    • Chetnani, B.1    Mondragón, A.2
  • 7
    • 1242274330 scopus 로고    scopus 로고
    • A guide to ions and RNA structure
    • D.E. Draper A guide to ions and RNA structure RNA 10 2004 335 343
    • (2004) RNA , vol.10 , pp. 335-343
    • Draper, D.E.1
  • 10
    • 77957111493 scopus 로고    scopus 로고
    • Use of the spliceosomal protein U1A to facilitate crystallization and structure determination of complex RNAs
    • A.R. Ferré-D'Amaré Use of the spliceosomal protein U1A to facilitate crystallization and structure determination of complex RNAs Methods 52 2010 159 167
    • (2010) Methods , vol.52 , pp. 159-167
    • Ferré-D'Amaré, A.R.1
  • 12
    • 80055093706 scopus 로고    scopus 로고
    • The roles of metal ions in regulation by riboswitches
    • A.R. Ferré-D'Amaré, and W.C. Winkler The roles of metal ions in regulation by riboswitches Met. Ions Life Sci. 9 2011 141 173
    • (2011) Met. Ions Life Sci. , vol.9 , pp. 141-173
    • Ferré-D'Amaré, A.R.1    Winkler, W.C.2
  • 14
    • 84876907659 scopus 로고    scopus 로고
    • T box RNA decodes both the information content and geometry of tRNA to affect gene expression
    • J.C. Grigg, Y. Chen, F.J. Grundy, T.M. Henkin, L. Pollack, and A. Ke T box RNA decodes both the information content and geometry of tRNA to affect gene expression Proc. Natl. Acad. Sci. USA 110 2013 7240 7245
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 7240-7245
    • Grigg, J.C.1    Chen, Y.2    Grundy, F.J.3    Henkin, T.M.4    Pollack, L.5    Ke, A.6
  • 15
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • W.A. Hendrickson, J.R. Horton, and D.M. LeMaster Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure EMBO J. 9 1990 1665 1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 16
    • 32944467057 scopus 로고    scopus 로고
    • Post-crystallization treatments for improving diffraction quality of protein crystals
    • B. Heras, and J.L. Martin Post-crystallization treatments for improving diffraction quality of protein crystals Acta Crystallogr. D Biol. Crystallogr. 61 2005 1173 1180
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 1173-1180
    • Heras, B.1    Martin, J.L.2
  • 17
    • 0033544719 scopus 로고    scopus 로고
    • Stitching together RNA tertiary architectures
    • T. Hermann, and D.J. Patel Stitching together RNA tertiary architectures J. Mol. Biol. 294 1999 829 849
    • (1999) J. Mol. Biol. , vol.294 , pp. 829-849
    • Hermann, T.1    Patel, D.J.2
  • 18
    • 33751299104 scopus 로고    scopus 로고
    • Sr(II) in water: A labile hydrate with a highly mobile structure
    • T.S. Hofer, B.R. Randolf, and B.M. Rode Sr(II) in water: A labile hydrate with a highly mobile structure J. Phys. Chem. B 110 2006 20409 20417
    • (2006) J. Phys. Chem. B , vol.110 , pp. 20409-20417
    • Hofer, T.S.1    Randolf, B.R.2    Rode, B.M.3
  • 20
    • 58249114463 scopus 로고    scopus 로고
    • Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA
    • A.V. Kazantsev, A.A. Krivenko, and N.R. Pace Mapping metal-binding sites in the catalytic domain of bacterial RNase P RNA RNA 15 2009 266 276
    • (2009) RNA , vol.15 , pp. 266-276
    • Kazantsev, A.V.1    Krivenko, A.A.2    Pace, N.R.3
  • 21
    • 34447260753 scopus 로고    scopus 로고
    • A general strategy to solve the phase problem in RNA crystallography
    • A.Y. Keel, R.P. Rambo, R.T. Batey, and J.S. Kieft A general strategy to solve the phase problem in RNA crystallography Structure 15 2007 761 772
    • (2007) Structure , vol.15 , pp. 761-772
    • Keel, A.Y.1    Rambo, R.P.2    Batey, R.T.3    Kieft, J.S.4
  • 22
    • 33748325570 scopus 로고    scopus 로고
    • Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
    • D.J. Klein, and A.R. Ferré-D'Amaré Structural basis of glmS ribozyme activation by glucosamine-6-phosphate Science 313 2006 1752 1756
    • (2006) Science , vol.313 , pp. 1752-1756
    • Klein, D.J.1    Ferré-D'Amaré, A.R.2
  • 23
    • 65649096161 scopus 로고    scopus 로고
    • Crystallization of the glmS ribozyme-riboswitch
    • D.J. Klein, and A.R. Ferré-D'Amaré Crystallization of the glmS ribozyme-riboswitch Methods Mol. Biol. 540 2009 129 139
    • (2009) Methods Mol. Biol. , vol.540 , pp. 129-139
    • Klein, D.J.1    Ferré-D'Amaré, A.R.2
  • 24
    • 34548591567 scopus 로고    scopus 로고
    • Requirement of helix P2.2 and nucleotide G1 for positioning the cleavage site and cofactor of the glmS ribozyme
    • D.J. Klein, S.R. Wilkinson, M.D. Been, and A.R. Ferré- D'Amaré Requirement of helix P2.2 and nucleotide G1 for positioning the cleavage site and cofactor of the glmS ribozyme J. Mol. Biol. 373 2007 178 189
    • (2007) J. Mol. Biol. , vol.373 , pp. 178-189
    • Klein, D.J.1    Wilkinson, S.R.2    Been, M.D.3    Ferré-D'Amaré, A.R.4
  • 25
    • 6044275739 scopus 로고    scopus 로고
    • Basis for structural diversity in homologous RNAs
    • A.S. Krasilnikov, Y. Xiao, T. Pan, and A. Mondragón Basis for structural diversity in homologous RNAs Science 306 2004 104 107
    • (2004) Science , vol.306 , pp. 104-107
    • Krasilnikov, A.S.1    Xiao, Y.2    Pan, T.3    Mondragón, A.4
  • 27
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 29
    • 0344142531 scopus 로고    scopus 로고
    • Crystal structure of acceptor stem of tRNA(Ala) from Escherichia coli shows unique G.U wobble base pair at 1.16 A resolution
    • U. Mueller, H. Schübel, M. Sprinzl, and U. Heinemann Crystal structure of acceptor stem of tRNA(Ala) from Escherichia coli shows unique G.U wobble base pair at 1.16 A resolution RNA 5 1999 670 677
    • (1999) RNA , vol.5 , pp. 670-677
    • Mueller, U.1    Schübel, H.2    Sprinzl, M.3    Heinemann, U.4
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 33749168652 scopus 로고    scopus 로고
    • Crystal structure of an RNA quadruplex containing inosine tetrad: Implications for the roles of NH2 group in purine tetrads
    • B. Pan, K. Shi, and M. Sundaralingam Crystal structure of an RNA quadruplex containing inosine tetrad: implications for the roles of NH2 group in purine tetrads J. Mol. Biol. 363 2006 451 459
    • (2006) J. Mol. Biol. , vol.363 , pp. 451-459
    • Pan, B.1    Shi, K.2    Sundaralingam, M.3
  • 34
    • 84861920270 scopus 로고    scopus 로고
    • Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch
    • A. Ren, K.R. Rajashankar, and D.J. Patel Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch Nature 486 2012 85 89
    • (2012) Nature , vol.486 , pp. 85-89
    • Ren, A.1    Rajashankar, K.R.2    Patel, D.J.3
  • 35
    • 84858964808 scopus 로고    scopus 로고
    • Increasing the X-ray Diffraction Power of Protein Crystals by Dehydration: The Case of Bovine Serum Albumin and a Survey of Literature Data
    • I. Russo Krauss, F. Sica, C.A. Mattia, and A. Merlino Increasing the X-ray Diffraction Power of Protein Crystals by Dehydration: The Case of Bovine Serum Albumin and a Survey of Literature Data Int. J. Mol. Sci. 13 2012 3782 3800
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 3782-3800
    • Russo Krauss, I.1    Sica, F.2    Mattia, C.A.3    Merlino, A.4
  • 37
    • 0037330568 scopus 로고    scopus 로고
    • Encapsulating streptomycin within a small 40-mer RNA
    • V. Tereshko, E. Skripkin, and D.J. Patel Encapsulating streptomycin within a small 40-mer RNA Chem. Biol. 10 2003 175 187
    • (2003) Chem. Biol. , vol.10 , pp. 175-187
    • Tereshko, V.1    Skripkin, E.2    Patel, D.J.3
  • 40
    • 53649104514 scopus 로고    scopus 로고
    • Structural basis for specific, high-affinity tetracycline binding by an in vitro evolved aptamer and artificial riboswitch
    • H. Xiao, T.E. Edwards, and A.R. Ferré-D'Amaré Structural basis for specific, high-affinity tetracycline binding by an in vitro evolved aptamer and artificial riboswitch Chem. Biol. 15 2008 1125 1137
    • (2008) Chem. Biol. , vol.15 , pp. 1125-1137
    • Xiao, H.1    Edwards, T.E.2    Ferré-D'Amaré, A.R.3
  • 41
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein
    • W. Yang, W.A. Hendrickson, R.J. Crouch, and Y. Satow Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein Science 249 1990 1398 1405
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4
  • 42
    • 84881665997 scopus 로고    scopus 로고
    • Co-crystal structure of a T-box riboswitch stem i domain in complex with its cognate tRNA
    • J. Zhang, and A.R. Ferré-D'Amaré Co-crystal structure of a T-box riboswitch stem I domain in complex with its cognate tRNA Nature 500 2013 363 366
    • (2013) Nature , vol.500 , pp. 363-366
    • Zhang, J.1    Ferré-D'Amaré, A.R.2
  • 43
    • 84903768300 scopus 로고    scopus 로고
    • Direct evaluation of tRNA aminoacylation status by the T-box riboswitch using tRNA-mRNA stacking and steric readout
    • J. Zhang, and A.R. Ferré-D'Amaré Direct evaluation of tRNA aminoacylation status by the T-box riboswitch using tRNA-mRNA stacking and steric readout Mol. Cell 55 2014 148 155
    • (2014) Mol. Cell , vol.55 , pp. 148-155
    • Zhang, J.1    Ferré-D'Amaré, A.R.2
  • 44
    • 84895751505 scopus 로고    scopus 로고
    • New molecular engineering approaches for crystallographic studies of large RNAs
    • J. Zhang, and A.R. Ferré-D'Amaré New molecular engineering approaches for crystallographic studies of large RNAs Curr. Opin. Struct. Biol. 26C 2014 9 15
    • (2014) Curr. Opin. Struct. Biol. , vol.26 C , pp. 9-15
    • Zhang, J.1    Ferré-D'Amaré, A.R.2
  • 45
    • 78049276834 scopus 로고    scopus 로고
    • Ribozymes and riboswitches: Modulation of RNA function by small molecules
    • J. Zhang, M.W. Lau, and A.R. Ferré-D'Amaré Ribozymes and riboswitches: modulation of RNA function by small molecules Biochemistry 49 2010 9123 9131
    • (2010) Biochemistry , vol.49 , pp. 9123-9131
    • Zhang, J.1    Lau, M.W.2    Ferré-D'Amaré, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.