Microgram-scale protein structure determination by NMR

被引:28
作者
Aramini, James M.
Rossi, Paolo
Anklin, Clemens
Xiao, Rong
Montelione, Gaetano T. [1 ]
机构
[1] Rutgers State Univ, Dept Mol Biol & Biochem, Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA
[2] Rutgers State Univ, NESG, Piscataway, NJ 08854 USA
[3] Bruker BioSpin Corp, Billerica, MA 01821 USA
[4] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Biochem & Mol Biol, Piscataway, NJ 08854 USA
关键词
D O I
10.1038/nmeth1051
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Using conventional triple-resonance nuclear magnetic resonance (NMR) experiments with a 1 mm triple-resonance microcoil NMR probe, we determined near complete resonance assignments and three-dimensional (3D) structure of the 68-residue Methanosarcina mazei TRAM protein using only 72 mu g (6 mu l, 1.4 mM) of protein. This first example of a complete solution NMR structure determined using microgram quantities of protein demonstrates the utility of microcoil-probe NMR technologies for protein samples that can be produced in only limited quantities.
引用
收藏
页码:491 / 493
页数:3
相关论文
共 11 条
[1]   Robotic cloning and Protein Production Platform of the Northeast Structural Genomics Consortium [J].
Acton, TB ;
Gunsalus, KC ;
Xiao, R ;
Ma, LC ;
Aramini, J ;
Baran, MC ;
Chiang, YW ;
Climent, T ;
Cooper, B ;
Denissova, NG ;
Douglas, SM ;
Everett, JK ;
Ho, CK ;
Macapagal, D ;
Rajan, PK ;
Shastry, R ;
Shih, LY ;
Swapna, GVT ;
Wilson, M ;
Wu, M ;
Gerstein, M ;
Inouye, M ;
Hunt, JF ;
Montelione, GT .
NUCLEAR MAGNETIC RESONANCE OF BIOLOGICAL MACROMOLECULES, PART C, 2005, 394 :210-243
[2]   Evaluating protein structures determined by structural genomics consortia [J].
Bhattacharya, Aneerban ;
Tejero, Roberto ;
Montelione, Gaetano T. .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2007, 66 (04) :778-795
[3]   Determination of regulatory phosphorylation sites in nanogram amounts of a synthetic fragment of ZAP-70 using microprobe NMR and on-line coupled capillary HPLC-NMR [J].
Hentschel, P ;
Krucker, M ;
Grynbaum, MD ;
Putzbach, K ;
Bischoff, R ;
Albert, K .
MAGNETIC RESONANCE IN CHEMISTRY, 2005, 43 (09) :747-754
[4]   A topology-constrained distance network algorithm for protein structure determination from NOESY data [J].
Huang, YJ ;
Tejero, R ;
Powers, R ;
Montelione, GT .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2006, 62 (03) :587-603
[5]   Protein NMR recall, precision, and F-measure scores (RPF scores):: Structure quality assessment measures based on information retrieval statistics [J].
Huang, YJ ;
Powers, R ;
Montelione, GT .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (06) :1665-1674
[6]   Micromixer-based time-resolved NMR: Applications to ubiquitin protein conformation [J].
Kakuta, M ;
Jayawickrama, DA ;
Wolters, AM ;
Manz, A ;
Sweedler, JV .
ANALYTICAL CHEMISTRY, 2003, 75 (04) :956-960
[7]   Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data [J].
Moseley, HNB ;
Monleon, D ;
Montelione, GT .
NUCLEAR MAGNETIC RESONANCE OF BIOLOGICAL MACROMOLECULES, PT B, 2001, 339 :91-108
[8]   Biomolecular NMR using a microcoil NMR probe - New technique for the chemical shift assignment of aromatic side chains in proteins [J].
Peti, W ;
Norcross, J ;
Eldridge, G ;
O'Neil-Johnson, M .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (18) :5873-5878
[9]  
Peti Wolfgang, 2005, Journal of Structural and Functional Genomics, V6, P259, DOI 10.1007/s10969-005-9000-x
[10]   High-resolution capillary tube NMR.: A miniaturized 5-μL high-sensitivity TXI probe for mass-limited samples, off-line LC NMR, and HT NMR [J].
Schlotterbeck, G ;
Ross, A ;
Hochstrasser, R ;
Senn, H ;
Kühn, T ;
Marek, D ;
Schett, O .
ANALYTICAL CHEMISTRY, 2002, 74 (17) :4464-4471