Related ArticlesTwo crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Biochemistry. 1994 Apr 19;33(15):4721-9
Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular replacement, based on the structure of the B2 domain (Brookhaven accession code 1PGX). Final R values are 0.174 and 0.198 for orthorhombic and trigonal forms, for diffraction data from 6.0 to 2.07 A and from 6 to 1.92 A, respectively. The orthorhombic crystals have an unusually high packing density for protein crystals, with Vm = 1.66 and a solvent content of 26%. The protein structure is found to be very similar (rms deviation 0.25 A for 56 C alpha's) in the two crystal forms, with an efficiently packed hydrophobic core between a four-stranded beta-sheet and a four-turn alpha-helix. The B1 domain has the same fold and general structure as the B2 domain (rms deviations 0.36 and 0.39 A), despite the six residue differences between them. The crystallographic models differ from NMR-derived models in several local regions, primarily in the loop involving residues 46-51; other significant variations are observed in the helix and in the structure of bound water. The primary crystal contact is the same in both crystal forms, involving both sheet edges to form extended beta-sheets throughout the crystals.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
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12-15-2010 12:03 PM
[NMR paper] Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Related Articles Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
J Am Chem Soc. 2005 Sep 7;127(35):12291-305
Authors: Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM
Magic-angle spinning...
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[NMR paper] NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M
NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
Related Articles NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
Biochemistry. 2004 Nov 9;43(44):13937-43
Authors: Pervushin K, Wider G, Iwai H, Wüthrich K
The N-terminal 63-residue fragment of the phage 434-repressor, 434(1-63), has a well-defined globular fold in H(2)O solution, and is unfolded in 6 M urea at pH 7.5. In this study, 434(1-63) has been refolded by adding either 1.7 M NaCl or 0.47 M NaTFA to the...
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Comparison of NMR and crystal structures highlights conformational isomerism in prote
Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.
Related Articles Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1393-405
Authors: Serrano P, Pedrini B, Geralt M, Jaudzems K, Mohanty B, Horst R, Herrmann T, Elsliger MA, Wilson IA, Wüthrich K
The JCSG has recently developed a protocol for systematic comparisons of high-quality crystal and NMR structures of proteins. In this...
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Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.
Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.
Related Articles Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1381-92
Authors: Mohanty B, Serrano P, Pedrini B, Jaudzems K, Geralt M, Horst R, Herrmann T, Elsliger MA, Wilson IA, Wüthrich K
The NMR structures of the TM1112 and TM1367 proteins from Thermotoga maritima in solution at 298 K were determined following a new protocol which uses the software package UNIO for...
[NMR paper] Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal prote
Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Related Articles Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Biochemistry. 1994 Apr 19;33(15):4721-9
Authors: Gallagher T, Alexander P, Bryan P, Gilliland GL
The structure of the 56-residue B1 immunoglobulin-binding domain from streptococcal protein G has been determined in two different crystal forms. The crystal structures were deduced by molecular...
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08-22-2010 03:33 AM
[NMR paper] 1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal prote
1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain.
Related Articles 1.67-A X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain.
Biochemistry. 1992 Nov 3;31(43):10449-57
Authors: Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M
The structure of the B2 immunoglobulin-binding domain of streptococcal protein G has been determined at 1.67-A...
Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal prote
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