Year |
Citation |
Score |
2019 |
Harrison K, Wu Z, Juers DH. A comparison of gas stream cooling and plunge cooling of macromolecular crystals. Journal of Applied Crystallography. 52: 1222-1232. PMID 31636524 DOI: 10.1107/S1600576719010318 |
0.348 |
|
2018 |
Juers DH, Farley CA, Saxby CP, Cotter RA, Cahn JKB, Holton-Burke RC, Harrison K, Wu Z. The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order. Acta Crystallographica. Section D, Structural Biology. 74: 922-938. PMID 30198901 DOI: 10.1107/S2059798318008793 |
0.361 |
|
2016 |
Juhasz MA, Matheson GR, Chang PS, Rosenbaum A, Juers DH. Microwave-Assisted Iodination: Synthesis of Heavily Iodinated 10-Vertex and 12-Vertex Boron Clusters Synthesis and Reactivity in Inorganic, Metal-Organic and Nano-Metal Chemistry. 46: 583-588. DOI: 10.1080/15533174.2014.988819 |
0.302 |
|
2014 |
Farley C, Juers DH. Efficient cryoprotection of macromolecular crystals using vapor diffusion of volatile alcohols. Journal of Structural Biology. 188: 102-6. PMID 25286441 DOI: 10.1016/J.Jsb.2014.09.011 |
0.364 |
|
2014 |
Farley C, Burks G, Siegert T, Juers DH. Improved reproducibility of unit-cell parameters in macromolecular cryocrystallography by limiting dehydration during crystal mounting. Acta Crystallographica. Section D, Biological Crystallography. 70: 2111-24. PMID 25084331 DOI: 10.1107/S1399004714012310 |
0.363 |
|
2012 |
Juers DH, Matthews BW, Huber RE. LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance. Protein Science : a Publication of the Protein Society. 21: 1792-807. PMID 23011886 DOI: 10.1002/Pro.2165 |
0.554 |
|
2012 |
Marshall H, Venkat M, Seng NS, Cahn J, Juers DH. The use of trimethylamine N-oxide as a primary precipitating agent and related methylamine osmolytes as cryoprotective agents for macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography. 68: 69-81. PMID 22194335 DOI: 10.1107/S0907444911050360 |
0.402 |
|
2011 |
Russi S, Juers DH, Sanchez-Weatherby J, Pellegrini E, Mossou E, Forsyth VT, Huet J, Gobbo A, Felisaz F, Moya R, McSweeney SM, Cusack S, Cipriani F, Bowler MW. Inducing phase changes in crystals of macromolecules: status and perspectives for controlled crystal dehydration. Journal of Structural Biology. 175: 236-43. PMID 21385612 DOI: 10.1016/J.Jsb.2011.03.002 |
0.345 |
|
2011 |
Juers DH, Marshall H, Venkat M. Investigations of Stabilizing Osmolytes as Precipitants for Protein Crystallization Biophysical Journal. 100: 312a. DOI: 10.1016/J.Bpj.2010.12.1902 |
0.363 |
|
2010 |
Alcorn T, Juers DH. Progress in rational methods of cryoprotection in macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography. 66: 366-73. PMID 20382989 DOI: 10.1107/S090744490903995X |
0.371 |
|
2009 |
Juers DH, Rob B, Dugdale ML, Rahimzadeh N, Giang C, Lee M, Matthews BW, Huber RE. Direct and indirect roles of His-418 in metal binding and in the activity of beta-galactosidase (E. coli). Protein Science : a Publication of the Protein Society. 18: 1281-92. PMID 19472413 DOI: 10.1002/Pro.140 |
0.524 |
|
2007 |
Juers DH, Lovelace J, Bellamy HD, Snell EH, Matthews BW, Borgstahl GE. Changes to crystals of Escherichia coli beta-galactosidase during room-temperature/low-temperature cycling and their relation to cryo-annealing. Acta Crystallographica. Section D, Biological Crystallography. 63: 1139-53. PMID 18007029 DOI: 10.1107/S0907444907045040 |
0.562 |
|
2005 |
Juers DH, Kim J, Matthews BW, Sieburth SM. Structural analysis of silanediols as transition-state-analogue inhibitors of the benchmark metalloprotease thermolysin. Biochemistry. 44: 16524-8. PMID 16342943 DOI: 10.1021/Bi051346V |
0.508 |
|
2004 |
Juers DH, Matthews BW. Cryo-cooling in macromolecular crystallography: advantages, disadvantages and optimization. Quarterly Reviews of Biophysics. 37: 105-19. PMID 15999418 DOI: 10.1017/S0033583504004007 |
0.538 |
|
2004 |
Juers DH, Matthews BW. The role of solvent transport in cryo-annealing of macromolecular crystals. Acta Crystallographica. Section D, Biological Crystallography. 60: 412-21. PMID 14993664 DOI: 10.1107/S0907444903027938 |
0.55 |
|
2003 |
Juers DH, Hakda S, Matthews BW, Huber RE. Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Biochemistry. 42: 13505-11. PMID 14621996 DOI: 10.1021/Bi035506J |
0.463 |
|
2003 |
Shoemaker GK, Juers DH, Coombs JM, Matthews BW, Craig DB. Crystallization of beta-galactosidase does not reduce the range of activity of individual molecules. Biochemistry. 42: 1707-10. PMID 12578385 DOI: 10.1021/Bi0204138 |
0.532 |
|
2001 |
Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry. 40: 14781-94. PMID 11732897 DOI: 10.1021/Bi011727I |
0.476 |
|
2001 |
Juers DH, Matthews BW. Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions. Journal of Molecular Biology. 311: 851-62. PMID 11518535 DOI: 10.1006/Jmbi.2001.4891 |
0.542 |
|
2000 |
Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW. High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Science : a Publication of the Protein Society. 9: 1685-99. PMID 11045615 DOI: 10.1110/Ps.9.9.1685 |
0.561 |
|
1999 |
Juers DH, Huber RE, Matthews BW. Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases. Protein Science : a Publication of the Protein Society. 8: 122-36. PMID 10210191 DOI: 10.1110/Ps.8.1.122 |
0.435 |
|
1995 |
Holland DR, Hausrath AC, Juers D, Matthews BW. Structural analysis of zinc substitutions in the active site of thermolysin. Protein Science : a Publication of the Protein Society. 4: 1955-65. PMID 8535232 DOI: 10.1002/Pro.5560041001 |
0.712 |
|
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