Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Pähler, A; Maslowska, M; Parge, HE; Schneider, M; Steifa, M; Saenger, W; Keuper, HJ; Spener, F.
X-ray studies on triclinic crystals of fatty acid binding protein. Examples of an extremely X-ray-resistant protein.
FEBS Lett. 1985; 184(2):185-187
Doi: 10.1016/0014-5793(85)80603-7
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- Co-Autor*innen der Med Uni Graz
- Spener Friedrich
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- Abstract:
- Fatty acid binding protein (pI 7.0) from bovine liver cytosol was crystallized using polyethylene glycol 4000 and 6000 as precipitating agents. The crystals are triclinic, space group P1. One molecule of 14 kDa occupies the unit cell with constants a = 33.5 A, b = 39.4 A, c = 30.6 A, alpha = 113.6 degrees, beta = 113.8 degrees, gamma = 88.8 degrees. Crystal diffraction extends to at least 2.25 A resolution and the crystals are stable in the X-ray beam for more than 450 h. One native data set to 2.5 A resolution has been collected.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Carrier Proteins -
- Cattle -
- Crystallography -
- Fatty Acid-Binding Proteins -
- Fatty Acids -
- Neoplasm Proteins -
- Protein Conformation -
- X-Ray Diffraction -