2a7d: Difference between revisions
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|PDB= 2a7d |SIZE=350|CAPTION= <scene name='initialview01'>2a7d</scene>, resolution 1.66Å | |PDB= 2a7d |SIZE=350|CAPTION= <scene name='initialview01'>2a7d</scene>, resolution 1.66Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7d OCA], [http://www.ebi.ac.uk/pdbsum/2a7d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a7d RCSB]</span> | |||
}} | }} | ||
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[[Category: Tucker, P A.]] | [[Category: Tucker, P A.]] | ||
[[Category: Weiss, M S.]] | [[Category: Weiss, M S.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:48:57 2008'' | ||
Revision as of 01:49, 31 March 2008
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| , resolution 1.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
OverviewOverview
Complete and highly redundant data sets were collected at different wavelengths between 0.80 and 2.65 A for a total of ten different protein and DNA model systems. The magnitude of the anomalous signal-to-noise ratio as assessed by the quotient R(anom)/R(r.i.m.) was found to be influenced by the data-collection wavelength and the nature of the anomalously scattering substructure. By utilizing simple empirical correlations, for instance between the estimated deltaF/F and the expected R(anom) or the data-collection wavelength and the expected R(r.i.m.), the wavelength at which the highest anomalous signal-to-noise ratio can be expected could be estimated even before the experiment. Almost independent of the nature of the anomalously scattering substructure and provided that no elemental X-ray absorption edge is nearby, this optimal wavelength is 2.1 A.
About this StructureAbout this Structure
2A7D is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:16131760
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