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Chunsun Zhang, Jinliang Xu, Wenli Ma, Wenling Zheng (2006)
PCR microfluidic devices for DNA amplification.Biotechnology advances, 24 3
B. Matthews (1968)
Solvent content of protein crystals.Journal of molecular biology, 33 2
A. Ragauskas, Charlotte Williams, B. Davison, George Britovsek, J. Cairney, C. Eckert, W. Frederick, J. Hallett, D. Leak, C. Liotta, J. Mielenz, R. Murphy, R. Templer, T. Tschaplinski (2006)
The Path Forward for Biofuels and BiomaterialsScience, 311
Chang Liu, Guangyu Yang, Lie Wu, G. Tian, Zuoming Zhang, Yan Feng (2011)
Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineeringProtein & Cell, 2
Yuguo Wang, Xiaonan Wang, Rentao Tang, Shanshan Yu, B. Zheng, Yan Feng (2010)
A novel thermostable cellulase from Fervidobacterium nodosumJournal of Molecular Catalysis B-enzymatic, 66
A. Mccoy, R. Grosse-Kunstleve, P. Adams, M. Winn, L. Storoni, R. Read (2007)
Phaser crystallographic softwareJournal of Applied Crystallography, 40
Y.‐H. Zhang, M. Himmel, J. Mielenz (2006)
Outlook for cellulase improvement: screening and selection strategies.Biotechnology advances, 24 5
E. Rubin (2008)
Genomics of cellulosic biofuelsNature, 454
Axel Brüngera, Paul Adamsb, G. Clorec, Warren DeLanod, Piet Grose, Ralf Grosse-Kunstlevea, Jian-Sheng Jiangf, John Kuszewskic, Michael Nilgesg, Navraj Pannuh, Randy Readi, Luke Riceb, Thomas Simonsonj, Gregory Warrenb (1998)
Crystallography & NMR system: A new software suite for macromolecular structure determination.Acta crystallographica. Section D, Biological crystallography, 54 Pt 5
Z. Otwinowski, W. Minor (1997)
[20] Processing of X-ray diffraction data collected in oscillation mode.Methods in enzymology, 276
M. Chang (2007)
Harnessing energy from plant biomass.Current opinion in chemical biology, 11 6
Jin-Man Kim, In-Soo Kong, Ju-Hyun Yu (1987)
Molecular cloning of an endoglucanase gene from an alkalophilic Bacillus sp. and its expression in Escherichia coliApplied and Environmental Microbiology, 53
Z. Lou, Ming Li, Yuna Sun, Ye Liu, Zheng Liu, Wenping Wu, Z. Rao (2010)
Crystal structure of a secreted lipase from Gibberella zeae reveals a novel “double-lock” mechanismProtein & Cell, 1
It is well known that protein cocrystallization is affected by several parameters such as the ratio of the protein to the ligand, the reservoir solution, the pH and the temperature. Previously, spatial blocking by the N‐terminus was observed in the active site in the crystal structure of the native protein of a thermostable endoglucanase from the thermophilic bacterium Fervidobacterium nodosum Rt17‐B1 (FnCel5A). It was speculated that the N‐terminal α‐helix might form interactions with the substrate‐binding residues and it was believed that this spatial block is special to some extent. In order to confirm the effect on cocrystallization, two N‐terminally truncated variants of FnCel5A were constructed, purified and cocrystallized at 291 K. A crystal of FnCel5AND_12–343 in complex with cellobiose was obtained using PEG 8000 as a precipitant. A 2.2 Å resolution data set was collected. This crystal form (space group P41212, unit‐cell parameters a = b = 47.3, c = 271.4 Å) differed from that of the native protein. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.05 Å3 Da−1.
Acta Crystallographica Section F – Wiley
Published: Oct 1, 2011
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