Zobrazeno 1 - 10
of 51
pro vyhledávání: '"Dariusch Hekmat"'
Controlling Protein Crystallization by Free Energy Guided Design of Interactions at Crystal Contacts
Autor:
Johannes Hermann, Daniel Bischoff, Phillip Grob, Robert Janowski, Dariusch Hekmat, Dierk Niessing, Martin Zacharias, Dirk Weuster-Botz
Publikováno v:
Crystals, Vol 11, Iss 6, p 588 (2021)
Protein crystallization can function as an effective method for protein purification or formulation. Such an application requires a comprehensive understanding of the intermolecular protein–protein interactions that drive and stabilize protein crys
Externí odkaz:
https://doaj.org/article/a0918a409a384a0492b47a34f5408640
Autor:
Phillip Nowotny, Dariusch Hekmat, Angela Krautenbacher, Johannes Hermann, Dirk Weuster-Botz, Kai Klöpfer, Jianing Li
Publikováno v:
Crystal Growth & Design. 19:2380-2387
Technical protein crystallization is an alternative to preparative chromatography for purification of proteins. However, only a few proteins are satisfactorily crystallizable for this technical pur...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::11a38ca9decf79c175c764451bf0df93
https://doi.org/10.1021/acs.cgd.9b00067
https://doi.org/10.1021/acs.cgd.9b00067
Controlling protein crystallization by free energy guided design of interactions at crystal contacts
Autor:
Dariusch Hekmat, Robert Janowski, Dierk Niessing, Johannes Hermann, Daniel Bischoff, Martin Zacharias, Dirk Weuster-Botz, Phillip Grob
Publikováno v:
Crystals 11:588 (2021)
Crystals
Volume 11
Issue 6
Crystals, Vol 11, Iss 588, p 588 (2021)
Crystals
Volume 11
Issue 6
Crystals, Vol 11, Iss 588, p 588 (2021)
Protein crystallization can function as an effective method for protein purification or formulation. Such an application requires a comprehensive understanding of the intermolecular protein–protein interactions that drive and stabilize protein crys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a71e5b213a598d886751420c8ccf612
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=62255
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=62255
Publikováno v:
Powder Technology. 320:213-222
During operation of packed-bed chromatography columns, the mechanical properties of the porous chromatographic particles determine the overall macroscopic compression behavior. The porous particles are biphasic materials consisting of a solid matrix
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::720046d86850d88f203b0690da857b41
https://doi.org/10.1016/j.powtec.2017.07.043
https://doi.org/10.1016/j.powtec.2017.07.043
Publikováno v:
Crystal Growth & Design. 17:4162-4169
A lab-scale stirred tank with a cooled tubular reactor in bypass was applied for continuous crystallization of lysozyme and a full-length therapeutic monoclonal antibody. The stirred tank was operated as a mixed suspension classified product removal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91495d03e310cffaccbf94939fe74ccf
https://doi.org/10.1021/acs.cgd.7b00436
https://doi.org/10.1021/acs.cgd.7b00436
Autor:
Dierk Niessing, Robert Janowski, Dariusch Hekmat, Dirk Weuster-Botz, Johannes Hermann, Phillip Grob, Brigitte Walla, Max Huber
Publikováno v:
Biotechnol. J. 15:2000010 (2020)
Technical crystallization is an attractive method to purify recombinant proteins. However, it is rarely applied due to the limited crystallizability of many proteins. To overcome this limitation, single amino acid exchanges are rationally introduced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2f31868ee07cfc16b2e807f4836dc49
https://mediatum.ub.tum.de/1546783
https://mediatum.ub.tum.de/1546783
The bioprocessing industry relies on packed-bed column chromatography as its primary separation process to attain the required high product purities and fulfill the strict requirements from regulatory bodies. Conventional column packing methods rely
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3bb84803abd5f775da5354c50e3d9a3
https://mediatum.ub.tum.de/doc/1580207/document.pdf
https://mediatum.ub.tum.de/doc/1580207/document.pdf
Publikováno v:
Journal of chromatography. A. 1590
A major limitation of the three-dimensional imaging of polymeric biochromatography particle packings using X-ray computed tomography is that the particles have a low density and a high porosity, making them almost undistinguishable from the surroundi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c09c20acb0a396fc2ea1ce63b3c4bf18
https://pubmed.ncbi.nlm.nih.gov/30638712
https://pubmed.ncbi.nlm.nih.gov/30638712
Autor:
Phillip Nowotny, Tobias E. Schrader, Dirk Weuster-Botz, Dariusch Hekmat, Johannes Hermann, Philipp Biggel
Publikováno v:
Acta Crystallogr F Struct Biol Commun
Lactobacillus brevis alcohol dehydrogenase (LbADH) is a well studied homotetrameric enzyme which catalyzes the enantioselective reduction of prochiral ketones to the corresponding secondary alcohols. LbADH is stable and enzymatically active at elevat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9edb286107696940f63ea075ab7019c
https://pubmed.ncbi.nlm.nih.gov/30511668
https://pubmed.ncbi.nlm.nih.gov/30511668
Publikováno v:
Biotechnology Letters. 37:1791-1801
To investigate quantitatively and reproducibly a scalable, preparative crystallization method in novel stirred tanks using three different protein solutions containing residual microbial host cell proteins (HCP). Lysozyme from solutions being spiked
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de972224138fc2f00be13f5b271087ac
https://doi.org/10.1007/s10529-015-1866-5
https://doi.org/10.1007/s10529-015-1866-5