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Biological Macromolecule Crystallization

GiUiland, G. L., Tung, M. and Ladner, J. E. (2002). The Biological Macromolecule Crystallization Database procedures and strategies. Acta Crystallogr. D 58,916-920. [Pg.261]

The process of crystallization is still largely a process of trial and error, but in an attempt to formulate general rules, the cumulative experiences of X-ray crystallographers are being compiled into online databases such as the Marseille Protein Crystallization Database (14) and the Biological Macromolecule Crystallization Database (15). These and similar databases will provide useful starting points in crystallization trials and may greatly accelerate the process. [Pg.2149]

Gilliland GL, Tung M, Blakeslee DM, Ladner JE. Biological macromolecule crystallization database, version-3.0 - New features, data and the NASA archive for protein crystal-growth data. Acta Cryst. D-Biol. Cryst. 1994 50 408-413. [Pg.2156]

G. L.Gilliland, M. Tung, D. M. Blakeslee, and J. Ladner, Biological Macromolecule Crystallization Database (BMCD), available online at http /A[Pg.496]

Gilliland, G. L. A biological macromolecule crystallization database a basis for a crystallization strategy. Crystal Growth 90, 51-59 (1988). [Pg.725]

Once crystals have been obtained, they must be isolated and prepared for X-ray crystal diffraction studies. This too is problematic, since biological macromolecule crystals are not the dense packed structures familiar to chemists used to working with small molecules. Rather,... [Pg.284]

For a completely accurate crystal structure determination. X-ray scattering must be observed and recorded by reflection from the vast majority of hfcHattice planes associated with a given biological macromolecule crystal. That is to say that an accurate structural determination is only possible if the vast majority of reciprocal lattice points can be sampled. In order to achieve this, the classical approach has been to use a device like a four-circle diffractometer (Figure 6.15) in which biological macromolecule crystals are first mounted in a goniometer head located at the centre of the diffractometer and then irradiated with an intense beam of X-rays, after which X-ray reflections may be observed sequentially, one at a time, in... [Pg.288]

Tel. 301-975-2208, fax 301-926-0416, e-mail rdj3 enh.nist.gov Thermodynamic data for almost 5000 gas phase compounds. Estimation of struaures drawn into program using Benson s additivity rules. IVTANTHERMO database with enthalpies of formation and other thermodynamic properties for 2300 substances. NIST/NASA/CARB Biological Macromolecule Crystallization Database with crystal growth conditions. PCs. [Pg.328]

Biological Macromolecule Crystallization xpdb.nist.gov 8060/BMCD4/index.faces Database BRENDA... [Pg.2658]

Biological Macromolecule Crystallization Database (BMCD) The Biological Macromolecule Crystallization Database (BMCD) contains crystal data and the crystallization conditions, which have been compiled from literature. These include proteins, protein.protein complexes, nucleic acid, nucleic acid nucleic acid complexes, protein nucleic acid complexes, and viruses. [Pg.990]

Biological Macromolecule Crystallization Database and the NASA Archive for Protein http //ibm4.carb.nist.gov 4400/... [Pg.2167]


See other pages where Biological Macromolecule Crystallization is mentioned: [Pg.19]    [Pg.341]    [Pg.419]    [Pg.2538]    [Pg.281]    [Pg.281]    [Pg.282]    [Pg.283]    [Pg.286]    [Pg.287]    [Pg.288]    [Pg.290]    [Pg.300]    [Pg.2694]    [Pg.700]    [Pg.2315]    [Pg.2472]   


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