Zobrazeno 1 - 7
of 7
pro vyhledávání: '"D. J. Manstein"'
Autor:
A. Meents, M. O. Wiedorn, V. Srajer, R. Henning, I. Sarrou, J. Bergtholdt, M. Barthelmess, P. Y. A. Reinke, D. Dierksmeyer, A. Tolstikova, S. Schaible, M. Messerschmidt, C. M. Ogata, D. J. Kissick, M. H. Taft, D. J. Manstein, J. Lieske, D. Oberthuer, R. F. Fischetti, H. N. Chapman
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Serial X-ray crystallography (SX) is used for data collection at X-ray Free Electron Lasers. Here the authors show that a polychromatic “pink” synchrotron X-ray beam can be used for SX, which is useful when crystal supply is limited and will allo
Externí odkaz:
https://doaj.org/article/cc4b957c6c4342de85d0699d4099bcd5
Publikováno v:
Nature structural biology. 8(3)
We combined protein engineering and single molecule measurements to directly record the step size of a series of myosin constructs with shortened and elongated artificial neck domains. Our results show that the step size has a clear linear dependence
Publikováno v:
Journal of molecular biology. 290(3)
Motifs N2 and N3, also referred to as switch-1 and switch-2, form part of the active site of molecular motors such as myosins and kinesins. In the case of myosin, N3 is thought to act as a gamma-phosphate sensor and moves almost 6 A relative to N2 du
Autor:
D J, Manstein
Publikováno v:
Symposia of the Society for Experimental Biology. 47
Cells undergo a wide variety of movements, such as directed locomotion, extension and retraction of cell surface projections, saltatory movement of intracellular particles and cytoplasmic streaming. These events involve changes in the organization an
Publikováno v:
Methods in enzymology. 196
Autor:
D J, Manstein, E F, Pai
Publikováno v:
The Journal of biological chemistry. 261(34)
The bifunctional enzyme FAD synthetase from Brevibacterium ammoniagenes was purified by a method involving ATP-affinity chromatography. The final preparation was more than 95% pure. The apparent molecular weight of the enzyme was determined as 38,000