Vote for your favorite mineral in #MinCup25! - Kosmochlor vs. Azurite
It's a battle of green vs blue as rare but vibrant chromium-bearing kosmochlor up against the deep blue copper alteration mineral azurite.
Log InRegister
Quick Links : The Mindat ManualThe Rock H. Currier Digital LibraryMindat Newsletter [Free Download]
Home PageAbout MindatThe Mindat ManualHistory of MindatCopyright StatusWho We AreContact UsAdvertise on Mindat
Donate to MindatCorporate SponsorshipSponsor a PageSponsored PagesMindat AdvertisersAdvertise on Mindat
Learning CenterWhat is a mineral?The most common minerals on earthInformation for EducatorsMindat ArticlesThe ElementsThe Rock H. Currier Digital LibraryGeologic Time
Minerals by PropertiesMinerals by ChemistryAdvanced Locality SearchRandom MineralRandom LocalitySearch by minIDLocalities Near MeSearch ArticlesSearch GlossaryMore Search Options
Search For:
Mineral Name:
Locality Name:
Keyword(s):
 
The Mindat ManualAdd a New PhotoRate PhotosLocality Edit ReportCoordinate Completion ReportAdd Glossary Item
Mining CompaniesStatisticsUsersMineral MuseumsClubs & OrganizationsMineral Shows & EventsThe Mindat DirectoryDevice SettingsThe Mineral Quiz
Photo SearchPhoto GalleriesSearch by ColorNew Photos TodayNew Photos YesterdayMembers' Photo GalleriesPast Photo of the Day GalleryPhotography

Brinkmann, C., Weiss, M. S., Weckert, E. (2006) The structure of the hexagonal crystal form of hen egg-white lysozyme. Acta Crystallographica Section D Biological Crystallography, 62 (4). 349-355 doi:10.1107/s0907444906000825

Advanced
   -   Only viewable:
Reference TypeJournal (article/letter/editorial)
TitleThe structure of the hexagonal crystal form of hen egg-white lysozyme
JournalActa Crystallographica Section D Biological Crystallography
AuthorsBrinkmann, C.Author
Weiss, M. S.Author
Weckert, E.Author
Year2006 (April 1)Volume62
Issue4
PublisherInternational Union of Crystallography (IUCr)
DOIdoi:10.1107/s0907444906000825Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID8477658Long-form Identifiermindat:1:5:8477658:7
GUID0
Full ReferenceBrinkmann, C., Weiss, M. S., Weckert, E. (2006) The structure of the hexagonal crystal form of hen egg-white lysozyme. Acta Crystallographica Section D Biological Crystallography, 62 (4). 349-355 doi:10.1107/s0907444906000825
Plain TextBrinkmann, C., Weiss, M. S., Weckert, E. (2006) The structure of the hexagonal crystal form of hen egg-white lysozyme. Acta Crystallographica Section D Biological Crystallography, 62 (4). 349-355 doi:10.1107/s0907444906000825
In(2006, April) Acta Crystallographica Section D Biological Crystallography Vol. 62 (4) International Union of Crystallography (IUCr)

See Also

These are possibly similar items as determined by title/reference text matching only.

Harata, Kazuaki, Akiba, Toshihiko (2006) Structural phase transition of monoclinic crystals of hen egg-white lysozyme. Acta Crystallographica Section D Biological Crystallography, 62 (4). 375-382 doi:10.1107/s0907444906001314
Weiss, Manfred S., Palm, Gottfried J., Hilgenfeld, Rolf (2000) Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD. Acta Crystallographica Section D Biological Crystallography, 56 (8). 952-958 doi:10.1107/s0907444900006685
Harata, Kazuaki, Akiba, Toshihiko (2004) Phase transition of triclinic hen egg-white lysozyme crystal associated with sodium binding. Acta Crystallographica Section D Biological Crystallography, 60 (4). 630-637 doi:10.1107/s0907444904001805
Yamada, Hiroyuki, Nagae, Takayuki, Watanabe, Nobuhisa (2015) High-pressure protein crystallography of hen egg-white lysozyme. Acta Crystallographica Section D Biological Crystallography, 71 (4). 742-753 doi:10.1107/s1399004715000292
Harata, K. (1994) X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules. Acta Crystallographica Section D Biological Crystallography, 50 (3). 250-257 doi:10.1107/s0907444993013290
Howell, P. L. (1995) Structure of hexagonal turkey egg-white lysozyme at 1.65Γ… resolution. Acta Crystallographica Section D Biological Crystallography, 51 (5). 654-662 doi:10.1107/s0907444994013612
Held, Jeanette, van Smaalen, Sander (2014) The active site of hen egg-white lysozyme: flexibility and chemical bonding. Acta Crystallographica Section D Biological Crystallography, 70 (4). 1136-1146 doi:10.1107/s1399004714001928
Cohen, G. H., Sheriff, S., Davies, D. R. (1996) Refined Structure of the Monoclonal Antibody HyHEL-5 with its Antigen Hen Egg-White Lysozyme. Acta Crystallographica Section D Biological Crystallography, 52 (2). 315-326 doi:10.1107/s0907444995014855
Thomas, B. R., Vekilov, P. G., Rosenberger, F. (1996) Heterogeneity Determination and Purification of Commercial Hen Egg-White Lysozyme. Acta Crystallographica Section D Biological Crystallography, 52 (4). 776-784 doi:10.1107/s090744499600279x
Walsh, Martin A., Schneider, Thomas R., Sieker, Larry C., Dauter, Zbigniew, Lamzin, Victor S., Wilson, Keith S. (1998) Refinement of Triclinic Hen Egg-White Lysozyme at Atomic Resolution. Acta Crystallographica Section D Biological Crystallography, 54 (4). 522-546 doi:10.1107/s0907444997013656
Thomas, B. R., Vekilov, P. G., Rosenberger, F. (1998) Effects of Microheterogeneity in Hen Egg-White Lysozyme Crystallization. Acta Crystallographica Section D Biological Crystallography, 54 (2). 226-236 doi:10.1107/s0907444997010676
 
and/or  
Mindat.org is an outreach project of the Hudson Institute of Mineralogy, a 501(c)(3) not-for-profit organization.
Copyright © mindat.org and the Hudson Institute of Mineralogy 1993-2025, except where stated. Most political location boundaries are Β© OpenStreetMap contributors. Mindat.org relies on the contributions of thousands of members and supporters. Founded in 2000 by Jolyon Ralph.
To cite: Ralph, J., Von Bargen, D., Martynov, P., Zhang, J., Que, X., Prabhu, A., Morrison, S. M., Li, W., Chen, W., & Ma, X. (2025). Mindat.org: The open access mineralogy database to accelerate data-intensive geoscience research. American Mineralogist, 110(6), 833–844. doi:10.2138/am-2024-9486.
Privacy Policy - Terms & Conditions - Contact Us / DMCA issues - Report a bug/vulnerability Current server date and time: September 9, 2025 23:16:02
Go to top of page