2g4x

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{{STRUCTURE_2g4x| PDB=2g4x | SCENE= }}
{{STRUCTURE_2g4x| PDB=2g4x | SCENE= }}
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'''Anomalous substructure od ribonuclease A (P3221)'''
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===Anomalous substructure od ribonuclease A (P3221)===
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==Overview==
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23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.
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(as it appears on PubMed at http://www.pubmed.gov), where 17327674 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17327674}}
==About this Structure==
==About this Structure==
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[[Category: Mueller-Dieckmann, C.]]
[[Category: Mueller-Dieckmann, C.]]
[[Category: Weiss, M S.]]
[[Category: Weiss, M S.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:40:40 2008''

Revision as of 17:40, 28 July 2008

Image:2g4x.png

Template:STRUCTURE 2g4x

Anomalous substructure od ribonuclease A (P3221)

Template:ABSTRACT PUBMED 17327674

About this Structure

2G4X is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths., Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674

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