메뉴 건너뛰기




Volumn 26, Issue 10, 2017, Pages 2098-2104

Neutron crystallographic studies of T4 lysozyme at cryogenic temperature

Author keywords

hydrogen; neutron; structure; T4 lysozyme; X ray

Indexed keywords

HYDROGEN; LYSOZYME; WATER;

EID: 85029637601     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.3231     Document Type: Article
Times cited : (20)

References (25)
  • 1
    • 0023104358 scopus 로고
    • Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution
    • Weaver LH, Matthews BW (1987) Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. J Mol Biol 193:189–199.
    • (1987) J Mol Biol , vol.193 , pp. 189-199
    • Weaver, L.H.1    Matthews, B.W.2
  • 3
    • 16644366044 scopus 로고    scopus 로고
    • Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods
    • Mooers BHM, Matthews BW (2004) Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods. Acta Cryst D60:1726–1737.
    • (2004) Acta Cryst , vol.D60 , pp. 1726-1737
    • Mooers, B.H.M.1    Matthews, B.W.2
  • 4
    • 33749080560 scopus 로고    scopus 로고
    • Neutron protein crystallography: current status and a brighter future
    • Myles DA (2006) Neutron protein crystallography: current status and a brighter future. Curr Opin Struct Biol 16:630–637.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 630-637
    • Myles, D.A.1
  • 5
    • 84949643086 scopus 로고    scopus 로고
    • Neutron protein crystallography: A complementary tool for locating hydrogens in proteins
    • O'Dell WB, Bodenheimer AM, Meilleur F (2016) Neutron protein crystallography: A complementary tool for locating hydrogens in proteins. Arch Biochem Biophys 602:48–60.
    • (2016) Arch Biochem Biophys , vol.602 , pp. 48-60
    • O'Dell, W.B.1    Bodenheimer, A.M.2    Meilleur, F.3
  • 6
    • 0024564552 scopus 로고
    • Control of enzyme activity by an engineered disulfide bond
    • Matsumura M, Matthews BW (1989) Control of enzyme activity by an engineered disulfide bond. Science 243:792–794.
    • (1989) Science , vol.243 , pp. 792-794
    • Matsumura, M.1    Matthews, B.W.2
  • 7
    • 85047675494 scopus 로고    scopus 로고
    • Protein release and foaming in Escherichia coli cultures grown in minimal medium
    • Törnkvist M, Larsson G, Enfors SO (1996) Protein release and foaming in Escherichia coli cultures grown in minimal medium. Bioprocess Eng 15:231–237.
    • (1996) Bioprocess Eng , vol.15 , pp. 231-237
    • Törnkvist, M.1    Larsson, G.2    Enfors, S.O.3
  • 8
    • 65649117362 scopus 로고    scopus 로고
    • Structural origin of weakly ordered nitroxide motion in spin-labeled proteins
    • Fleissner MR, Cascio D, Hubbell WL (2009) Structural origin of weakly ordered nitroxide motion in spin-labeled proteins. Protein Sci 18:893–908.
    • (2009) Protein Sci , vol.18 , pp. 893-908
    • Fleissner, M.R.1    Cascio, D.2    Hubbell, W.L.3
  • 9
    • 0015925846 scopus 로고
    • Crystallographic data for lysozyme from bacteriophage T4
    • Matthews BW, Dahlquist FW, Maynard AY (1973) Crystallographic data for lysozyme from bacteriophage T4. J Mol Biol 78:575–576.
    • (1973) J Mol Biol , vol.78 , pp. 575-576
    • Matthews, B.W.1    Dahlquist, F.W.2    Maynard, A.Y.3
  • 10
    • 84864207317 scopus 로고    scopus 로고
    • Neutron protein crystallography at ultra-low (<15 K) temperatures
    • Myles DAA, Dauvergne F, Blakeley MP, Meilleur F (2012) Neutron protein crystallography at ultra-low (<15 K) temperatures. J Appl Cryst 45:686–692.
    • (2012) J Appl Cryst , vol.45 , pp. 686-692
    • Myles, D.A.A.1    Dauvergne, F.2    Blakeley, M.P.3    Meilleur, F.4
  • 12
    • 0025234587 scopus 로고
    • pH-Induced denaturation of proteins: a single salt bridge contributes 3–5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson DE, Becktel WJ, Dahlquist FW (1990) pH-Induced denaturation of proteins: a single salt bridge contributes 3–5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29:2403–2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 15
    • 0023660935 scopus 로고
    • Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157- Ile
    • Grütter MG, Gray TM, Weaver LH, Alber T, Wilson K, Matthews BW (1987) Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157- Ile. J Mol Biol 197:315–329.
    • (1987) J Mol Biol , vol.197 , pp. 315-329
    • Grütter, M.G.1    Gray, T.M.2    Weaver, L.H.3    Alber, T.4    Wilson, K.5    Matthews, B.W.6
  • 16
    • 0028341789 scopus 로고
    • Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme
    • Zhang X-J, Matthews BW (1994) Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme. Protein Sci 3:1031–1039.
    • (1994) Protein Sci , vol.3 , pp. 1031-1039
    • Zhang, X.-J.1    Matthews, B.W.2
  • 17
    • 55749086402 scopus 로고    scopus 로고
    • Use of experimental crystallographic phases to examine the hydration of polar and nonpolar cavities in T4 lysozyme
    • Liu L, Quillin ML, Matthews BW (2008) Use of experimental crystallographic phases to examine the hydration of polar and nonpolar cavities in T4 lysozyme. Proc Natl Acad Sci USA 105:14406–14411.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14406-14411
    • Liu, L.1    Quillin, M.L.2    Matthews, B.W.3
  • 18
    • 70350787183 scopus 로고    scopus 로고
    • Deuterium labeling for neutron structure-function-dynamics analysis
    • Meilleur F, Weiss KL, Myles DAA (2009) Deuterium labeling for neutron structure-function-dynamics analysis. Methods Mol Biol 544:281–292.
    • (2009) Methods Mol Biol , vol.544 , pp. 281-292
    • Meilleur, F.1    Weiss, K.L.2    Myles, D.A.A.3
  • 25
    • 85029636660 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Version 1.8
    • Schrodinger LLC (2015) The PyMOL Molecular Graphics System, Version 1.8.
    • (2015)
    • Schrodinger, L.L.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.