We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2qmt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qmt.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qmt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qmt| PDB=2qmt | SCENE= }}
{{STRUCTURE_2qmt| PDB=2qmt | SCENE= }}
-
'''Crystal Polymorphism of Protein GB1 Examined by Solid-state NMR and X-ray Diffraction'''
+
===Crystal Polymorphism of Protein GB1 Examined by Solid-state NMR and X-ray Diffraction===
-
==Overview==
+
<!--
-
The study of micro- or nanocrystalline proteins by magic-angle spinning (MAS) solid-state NMR (SSNMR) gives atomic-resolution insight into structure in cases when single crystals cannot be obtained for diffraction studies. Subtle differences in the local chemical environment around the protein, including the characteristics of the cosolvent and the buffer, determine whether a protein will form single crystals. The impact of these small changes in formulation is also evident in the SSNMR spectra; however, the changes lead only to correspondingly subtle changes in the spectra. Here, we demonstrate that several formulations of GB1 microcrystals yield very high quality SSNMR spectra, although only a subset of conditions enable growth of single crystals. We have characterized these polymorphs by X-ray powder diffraction and assigned the SSNMR spectra. Assignments of the 13C and 15N SSNMR chemical shifts confirm that the backbone structure is conserved, indicative of a common protein fold, but side chain chemical shifts are changed on the surface of the protein, in a manner dependent upon crystal packing and electrostatic interactions with salt in the mother liquor. Our results demonstrate the ability of SSNMR to reveal minor structural differences among crystal polymorphs. This ability has potential practical utility for studying the formulation chemistry of industrial and therapeutic proteins, as well as for deriving fundamental insights into the phenomenon of single-crystal growth.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18052145}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18052145 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18052145}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Immunglobulin binding domain]]
[[Category: Immunglobulin binding domain]]
[[Category: Thermostable]]
[[Category: Thermostable]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:13:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:53:39 2008''

Revision as of 04:53, 29 July 2008

Image:2qmt.png

Template:STRUCTURE 2qmt

Crystal Polymorphism of Protein GB1 Examined by Solid-state NMR and X-ray Diffraction

Template:ABSTRACT PUBMED 18052145

About this Structure

2QMT is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction., Schmidt HL, Sperling LJ, Gao YG, Wylie BJ, Boettcher JM, Wilson SR, Rienstra CM, J Phys Chem B. 2007 Dec 27;111(51):14362-9. Epub 2007 Dec 4. PMID:18052145

Page seeded by OCA on Tue Jul 29 07:53:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qmt"
Personal tools