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 Center for Biotechnology and Biomedicine
 Institute of Bioanalytical Chemistry
  Structural analysis of biopolymers
  Prof. Dr. Norbert Sträter



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S. Bhattarai, J. Pippel, E. Scaletti, R. Idris, M. Freundlieb, G. Rolshoven, C. Renn, SY Lee,  A. Abdelrahman, H. Zimmermann, A. El-Tayeb, CE Müller, N. Sträter      
2-Substituted α,β-Methylen -ADP Derivatives: Potent Competitive Ecto-5'-nucleotidase (CD73) Inhibitors with Variable Binding Modes
J. Med Chem. 2020, 63 (6): 2941-2957.

S. Bhattarai, J. Pippel, A. Meyer, M. Freundlieb, C. Schmies, A. Abdelrahman et al.      
X-Ray Co-Crystal Structure Guides the Way to Subnanomolar Competitive Ecto-5'-Nucleotidase (CD73) Inhibitors for Cancer Immunotherapy 
Advanced Therapeutics 2019, 2 (10), 1900075.

M. Zahn, N. Kurteva-Yaneva, J. Schuster, U. Krug, T. Georgi, R. Müller, T. Rohwerder and N.Sträter
Structures of 2-hydroxyisobutyric acid-CoA ligase reveal determinants of substrate specificity and describe a multi-conformational catalytic cycle
J. Mol. Biol. 2019, 431(15):2747-2761.

C. Döhler, M. Zebisch, D. Krinke, A. Robitzki, N. Sträter

Crystallization of ectonucleotide phosphodiesterase/pyrophosphatase-3 and orientation of the SMB domains in the full-length ectodomain
Acta Crystallogr. F Struct. Biol. Commun. 2018, 74: 696-703.

C. Döhler, M. Zebisch, N. Sträter
Crystal structure and substrate binding mode of ectonucleotide phosphodiesterase/pyrophosphatase-3 (NPP3)
Sci. Rep.  2018, 8: 10874.

D. Ulbricht, CA. Tindall, K. Oertwig, S. Hanke, N. Sträter, JT. Heiker
Kallikrein-related peptidase 14 is the second KLK protease targeted by the serpin vaspin
Biol. Chem.  2018, 399:1079-1084.

K. Oertwig, D. Ulbricht, S. Hanke, J. Pippel, K. Bellmann-Sickert, N. Sträter, JT. Heiker
Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability
Biochim. Biophys. Acta  2017, 1865(9):1188-1194.

C. Roth, N. Weizenmann, N. Bexten, W. Saenger, W. Zimmermann, T. Maier, N. Sträter
Amylose recognition and ring-size determination of amylomaltase
Sci. Adv. 2017, 13;3(1):e1601386 doi: 10.1126/sciadv.1601386

D. Ulbricht, K. Oertwig, K. Arnsburg, A. Saalbach, J. Pippel, N. Sträter, JT. Heiker

Basic Residues of ß-Sheet A Contribute to Heparin Binding and Activation of Vaspin  (Serpin A12)
J. Biol. Chem. 2017, 292, 994-1004.

D. Arac, N. Sträter, E. Seiradake

Understanding the Structural Basis of Adhesion GPCR Functions
Handb. Exp. Pharmacol.  2016, 234, 67-82.

T.M. Kriegel, K. Kettner, G. Rödel, N. Sträter
Regulatory Function of Hexokinase 2 in Glucose Signaling in Saccharomyces cerevisiae
J. Biol. Chem. 2016, 291, 16477.

D. Knappe, T. Goldbach, M.P Hatfield, N.Y. Palermo, S. Weinert, N. Sträter, R. Hoffmann,
S. Lovas

Proline-rich Antimicrobial Peptides Optimized for Binding to Escheria coli Chaperone DnaK
Protein Pept. Lett. 2016, 23, 1061-1071.

U. Krug, N.S. Alexander, R.A. Stein, A. Keim, H.S. Mchaourab, N. Sträter, J. Meiler
Characterization of the Domain Orientations of E. coli 5'-Nucleotidase by Fitting an Ensemble of Conformers to DEER Distance Distributions
Structure 2016, 24, 43-56.

J. Pippel, E.B. Küttner, D. Ulbricht, J. Daberger, S. Schultz, J.T. Heiker, N. Sträter
Crystal structure of cleaved vaspin (serpinA12)
Biol. Chem. 2016, 397, 111-23

D. Ulbricht, J. Pippel, S. Schultz, R. Meier, N. Sträter, J.T. Heiker

A unique serpin P1' glutamate and a conserved β-sheet C arginine are key residues for activity, protease recognition and stability of serpinA12 (vaspin)
Biochem. J. 2015, 470, 357-367.

M. Kloos, A. Brüser, J. Kirchberger, T. Schöneberg, N. Sträter
Crystal structure of human platelet phosphofructokinase-1 locked in an activated conformation 
Biochem. J. 2015, 469, 421-432.

S. Bhattarai, M. Freundlieb, J. Pippel, A. Meyer, A. Abdelrahman, A. Fiene, S.Y. Lee, H. Zimmermann, G.G. Yegutkin, N. Sträter, A. El-Tayeb, C.E. Müller

α,β-Methylene-ADP (AOPCP) Derivatives and Analogues: Development of Potent and Selective ecto-5'-Nucleotidase (CD73) Inhibitors
J. Med. Chem. 2015, 58, 6248-6263.

N. Kurteva-Yaneva, M. Zahn, M. T. Weichler, R. Starke, H. Harms, R. H. Müller, N. Sträter, T. Rohwerder
Structural Basis of the Stereospecificity of Bacterial B12-dependent 2-Hydroxyisobutyryl-CoA Mutase
J. Biol. Chem. 2015, 290, 9727-9737.

K. Buettner, T. Kreisig, N. Sträter, T. Zuchner
Protein surface charge of trypsinogen changes its activation pattern
BMC Biotechnol. 2014, 14, 109.

A. Krizsan, D. Volke, S. Weinert, N. Sträter, D. Knappe, R. Hoffmann
Insect-Derived Proline-Rich Antimicrobial Peptides Kill Bacteria by Inhibiting Bacterial Protein Translation at the 70 S Ribosome
Angew Chem Int Ed Engl 2014, 53, 12236-12239.

M. Genz, N. Sträter
Posttranslational Incorporation of Non-canonical Amino Acids in the RNase S System by Semisynthetic Protein Assembly
Methods Mol. Biol. 2014, 1216, 71-87.

M. Kloos, A. Brüser, J. Kirchberger, T. Schöneberg, N. Sträter
Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis
Acta Cryst. F 2014, 70, 578-582.

G. Schwan, G. Barbar Asskar, N. Höfgen, L. Kubicova, U. Funke, U. Egerland, M. Zahn, K. Nieber, M. Scheunemann, N. Sträter, P. Brust, D. Briel
Fluorine-Containing 6,7-Dialkoxybiaryl-Based Inhibitors for Phosphodiesterase 10A: Synthesis and in vitro Evaluation of Inhibitory Potency, Selectivity, and Metabolism
ChemMedChem 2014, 9, 1476-1487.

C. Roth, R. Wei, T. Oeser, J. Then, C. Föllner, W. Zimmermann, N. Sträter
Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca
Appl. Microbiol. Biotechnol. 2014, 98, 7815-7823.

M. Zebisch, M. Krauss, P. Schäfer, N. Sträter
Structures of Legionella pneumophila NTPDase1 in complex with polyoxometallates
Acta Cryst. D 2014, 70, 1147-1154.

M. Genz, V. Köhler, M. Krauss, D. Singer, R. Hoffmann, T. Ward, N. Sträter
An Artificial Imine Reductase based on the Ribonuclease S Scaffold
ChemCatChem 2014, 6, 736-740.

M. Zebisch, Y. Baqi, P. Schäfer, C. E. Müller, N. Sträter
Crystal structure of NTPDase2 in complex with the sulfoanthraquinone inhibitor PSB-071
J. Struct. Biol. 2014, 185, 336-341.

M. Zahn, B. Kieslich, N. Berthold, D. Knappe, R. Hoffmann, N. Sträter
Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7

Prot. Pept. Lett.
2014, 21, 407-412.

M. Genz, D. Singer, E. Hey-Hawkins, R. Hoffmann, N. Sträter

Crystal Structure of Apo- and Metalated Thiolate containing RNase S as Structural Basis for the Design of Artificial Metalloenzymes by Peptide-Protein Complementation
Z. Anorg. Allg. Chem.
2013, 639, 2395-2400.

U. Krug, R. Totzauer, M. Zebisch, N. Sträter
The ATP/ADP Substrate Specificity Switch between Toxoplasma gondii NTPDase1 and NTPDase3 is Caused by an Altered Mode of Binding of the Substrate Base
2013, 14, 2292-2300.

M. Zebisch, M. Krauss, P. Schäfer, P.Lauble, N. Sträter
Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases

2013, 21, 1460-1475.

J. Breitfeld, J. T. Heiker, Y. Böttcher, D. Schleinitz, A. Tönjes, K. Weidle, K. Krause, E. B. Küttner, M. Scholz, W. Kiess, N. Sträter, A. G. Beck-Sickinger, M. Stumvoll, A. Körner, M. Blüher, P. Kovacs
Analysis of a rare functional truncating mutation rs61757459 in vaspin (SERPINA12) on circulating vaspin levels
J. Mol. Med. 2013, 91, 1285-1292.
T. Schöneberg, M. Kloos, A. Brüser, J. Kirchberger, N. Sträter
Structure and allosteric regulation of eukaryotic 6-phosphofructokinases

Biological Chemistry
2013, 394, 977-993.

K. Kettner, E. B. Küttner, A. Otto, H. Lilie, R. P. Golbik, N. Sträter, T. M. Kriegel
In vivo phosphorylation and in vitro autophosphorylation-inactivation of Kluyveromyces lactis hexokinase KlHxk1

Biochem. Biophys. Res. Comm.
2013, 435, 313-318.

M. Zahn, N. Berthold, B. Kieslich, D. Knappe, R. Hoffmann, N. Sträter
Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK
J. Mol. Biol. 2013, 425, 2463-2479.

U. Krug, R. Totzauer, N. Sträter
The crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 represents a conformational intermediate in the reductive activation mechanism of the tetrameric enzyme
Proteins 2013, 81, 1271-1276.

M. Zebisch, P. Schäfer, P. Lauble, N. Sträter
New crystal forms of NTPDase1 from the bacterium Legionella pneumophila
Acta Cryst. F 2013, 69, 259-262.

C. Roth, A. D. Janosch, S. R. Kaschabek, M. Schlömann, N. Sträter
Crystal structure and catalytic mechanism of chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1CP

Mol. Microbiol.
2013, 88, 254-267.

S. O. Dahms, M. Kuester, C. Streb, C. Roth, N. Sträter, M. E. Than
Localization and orientation of heavy-atom cluster compounds in protein crystals using molecular replacement
Acta Cryst. D
2013, 69, 284-297.

J. T. Heiker, N. Klöting, P. Kovacs, E. B. Küttner, N. Sträter, S. Schultz, M. Kern, M. Stumvoll, M. Blüher, A. G. Beck-Sickinger
Vaspin inhibits kallikrein 7 by serpin mechanism
Cell. Mol. Life Sci. 2013, 70, 2569-2583.

U. Krug, R. Patzschke, M. Zebisch, J. Balbach, N. Sträter
Contribution of the two domains of E. coli 5'-nucleotidase to substrate specificity and catalysis
FEBS Lett. 2013, 587, 460-466.

K. M. Knapp, M. Zebisch, N. Sträter
Crystallization and preliminary X-ray analysis of the open form of human ecto-5'-nucleotidase (CD73)
Acta Cryst. Sect. F 2012, 68, 1545-1549.

K. Knapp, M. Zebisch, J. Pippel, A. El-Tayeb, C. E. Müller, N. Sträter
Crystal Structure of the Human Ecto-5'-Nucleotidase (CD73): Insights into the Regulation of Purinergic Signaling
Structure 2012, 20, 2161-2173.

J. A. Gröning, C. Roth, S. R. Kaschabek, N. Sträter, M. Schlömann
Recombinant expression of a unique chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1CP and identification of catalytically relevant residues by mutational analysis.
Arch. Biochem. Biophys. 2012, 526, 69-77.

C. Roth, S. R. Kaschabek, J. A. Gröning, T. Handrek, M. Schlömann, N. Sträter
Crystallization and preliminary characterization of chloromuconolactone dehalogenase from Rhodococcus opacus 1CP.
Acta Cryst. Sect. F 2012, 68, 591-595.

P. Czihal, D. Knappe, S. Fritsche, M. Zahn, N. Berthold, S. Piantavigna, U. Müller, S. van Dorpe, N. Herth, A. Binas, G. Köhler, B. de Spiegeleer, L. L. Martin, O. Nolte, N. Sträter, G. Alber, R. Hoffmann
Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant gram-negative pathogens.
ACS Chem. Biol. 201271281-1291.

H. Zimmermann, M. Zebisch, N. Sträter 
Cellular function and molecular structure of ecto-nucleotidases.
Purinergic Signal. 20128, 437-502.

P. Simeonov, M. Zahn, N. Sträter, T. Zuchner
Crystal structure of a supercharged variant of the human enteropeptidase light chain.
Proteins 201280, 1907-1910.

A. Brüser, J. Kirchberger, M. Kloos, N. Sträter, T. Schöneberg
Functional linkage of adenine nucleotide binding sites in mammalian muscle 6-phosphofructokinase.
J. Biol. Chem. 2012, 287, 17546-17553.

U. Krug, M. Zebisch, M. Krauss, N. Sträter
Structural insight into activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase by disulfide reduction
J. Biol. Chem. 2012, 287, 3051-3066.

M. Zebisch, M. Krauss, P. Schäfer, N. Sträter
Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase)1
J. Mol. Biol. 2012, 415, 288-306.

D. Knappe, M. Zahn, U. Sauer, G. Schiffer, N. Sträter, R. Hoffmann
Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structures of the oncocin-DnaK complex
Chembiochem. 2011, 12, 874-876.

P. Simeonov, R. Berger-Hoffmann, R. Hoffmann, N. Sträter, T. Zuchner
Surface supercharged human enteropeptidase light chain shows improved solubility and refolding yield.
Protein Eng. Des. Sel.  2011, 24, 261-268.

E. B. Kuettner, K. Kettner, A. Keim, D. I. Svergun, D. Volke, S. Singer, R. Hoffmann, E. C. Müller, A. Otto, T. M. Kriegel, N. Sträter
Crystal structure of hexokinase KlHxk1 of Kluyveromyces lactis: a molecular basis for understanding the control of yeast hexokinase functions via covalent modification and oligomerization
J. Biol. Chem. 2010, 285, 41019-41033.

N. Sträter, S. Marek, E. B. Kuettner, M. Kloos, A. Keim, A. Brüser, J. Kirchberger, T. Schöneberg
Molecular architecture and structural basis of allosteric regulation of eukaryotic phosphofructokinases.
FASEB J. 2011, 25, 89-95.

R. Schmiedel, E. B. Kuettner, A. Keim, N. Sträter, T. Greiner-Stöffele
Structure and function of the abasic site specificity pocket of an AP endonuclease from Archaeoglobus fulgidus
DNA Repair  20098, 219-231.

M. Q. Müller, C. Roth, N. Sträter, A. Sinz
Expression and purification of the ligand-binding domain of peroxisome proliferator-activated receptor alpha (PPAR
Protein Expression and Purification 2008, 62, 185-189.

M. Zebisch, N. Sträter
Structural basis of signal conversion and inactivation by NTPDase2 in purinergic signalling
Proc. Natl. Acad. Sci. USA 2008, 105, 6882-6887.

E. B. Kuettner, A. Keim, M. Kirchner, S. Rosmus, N. Sträter
Active site mobility revealed by the crystal structure of arylmalonate decarboxylase from Bordetella bronchisepticus
J. Mol. Biol. 2008,
377, 386-394.

K. S. Paithankar, C. Feller, E. B. Kuettner, A. Keim, M. Grunow, N. Sträter
Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida
FEBS J. 2007, 274, 5767-5779.

M. Zebisch, N. Sträter
Characterisation of rat NTPDase1, -2 and -3 ectodomains refolded from bacterial inclusion bodies
Biochemistry 2007, 46, 11945-11956.

E. B. Kuettner, T. M. Kriegel, A. Keim, M. Naumann, N. Sträter
Crystallization and preliminary X-ray diffraction studies of hexokinase KlHxk1 from Kluyveromyces lactis
Acta Cryst. Sect. F 2007, 63, 430-433.

E. B. Kuettner, S. Pfeifer, A. Keim, T. Greiner-Stöffele, N. Sträter
Crystallization and preliminary X-ray characterization of two thermostable DNA nucleases
Acta Cryst. Sect. F 2006, 62, 1290-1293.

N. Sträter
Ecto-5'-Nucleotidase: Structure Function Relationships
Purinergic Signalling 2006, 2, 343-350.

N. Sträter, B. Jasper, M. Scholte, B. Krebs, A. P. Duff, D. B. Langley, R. Han, B. A. Averill, H. C. Freeman, J. M. Guss
Crystal structures of recombinant human purple acid phosphatase with and without an inhibitory conformation of the repression loop
J. Mol. Biol. 2005, 351, 233-246.

T. Maier, I. Przylas, N. Sträter, P. Herdewijn, W. Saenger
Reinforced HNA backbone hydration in the crystal structure of a decameric HNA/RNA hybrid
J. Am. Chem. Soc. 2005, 127, 2937-2943

R. Schultz-Heienbrok, T. Maier, N. Sträter
A Large Hinge Bending Domain Rotation is Required for the Catalytic Function of E. coli 5'-Nucleotidase
Biochemistry 2005, 44, 2244-2252.

N. Sträter and W. N. Lipscomb
Leucyl aminopeptidase (animal)
in Handbook of proteolytic enzymes, 2nd ed., pp. 896-901, Ed. A. J. Barrett, N. D. Rawlings, J. F. Woessner, Elsevier, New York, 2004.

R. Schultz-Heienbrok, T. Maier, N. Sträter
Trapping a 96° domain rotation in two distinct conformations by engineered disulfide bridges
Protein Science 2004, 13, 1811-1822.

N. Sträter, T. Maier
Proteinkristallographie im Zeitalter der Strukturgenomik (Trendbericht Biochemie und Molekularbiologie 2003)
Nachr. Chem. 2004, 52, 292-297.

N. Sträter, W. N. Lipscomb
Leucine aminopeptidase
in Handbook of Metalloproteins Vol. 3, pp. 199-207, Eds. A. Messerschmidt, W. Bode, M. Cygler, Wiley, Chichester, 2004.

N. Sträter
in Handbook of Metalloproteins Vol. 3, pp. 62-70, Eds. A. Messerschmidt, W. Bode, M. Cygler, Wiley, Chichester, 2004.

R. Czaja, M. Struhalla, K. Hoschler, W. Saenger, N. Sträter, U. Hahn
RNase T1 variant RV cleaves single-stranded RNA after purines due to specific recognition by the Asn46 side chain amide
Biochemistry 2004, 43, 2854-2862.

H. Xu, N. Sträter, W. Schröder, C. Bottcher, K. Ludwig, W. Saenger
Structure of DNA helicase RepA in complex with sulfate at 1.95 A resolution implicates structural changes to an 'open' form
Acta Crystallogr Sect. D 2003, 59, 815-822.

J.A. Lodge, T. Maier, W. Liebl, V. Hoffmann and N. Sträter
Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases
J. Biol. Chem. 2003, 278, 19151-19158.

T. Maier, N. Sträter, C. Schuette, R. Klingenstein, K. Sandhoff, W. Saenger
The X-ray crystal structure of human
b-hexosaminidase B provides new insights into Sandhoff disease
J. Mol. Biol. 2003, 328, 669-681.

A. Meinhart, J.C. Alonso, N. Sträter and W. Saenger
Crystal structure of the plasmid maintenance system
e/z : Functional mechanism of toxin z and inactivation by e2/z2 complex formation
Proc Natl Acad Sci U S A 2003,100,1661-1666.

C. Raasch, M. Armbrecht, W. Streit,  B. Höcker, N. Sträter and W. Liebl
Identification of residues important for NAD+ binding by the Thermotoga maritima a
glucosidase AglA, a member of the glycoside hydrolase family 4

FEBS Letters 2002, 517, 267-271.

N. Sträter, I. Przylas, W. Saenger, Y. Terada, K. Fuji and T. Takaha
Structural basis of the synthesis of large cycloamyloses by amylomaltase
Biologia Bratislava 2002, 57
, 93-99.

T. Knöfel and N. Sträter
Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures
J. Mol. Biol. 2001, 309, 239-254.

A. Meinhart, C. Alings, N. Sträter, A. G. Camacho, J. C. Alonso and W. Saenger
Crystallization and preliminary X-ray diffraction studies of the
ez addiction system encoded by Streptococcus pyogenes plasmid pSM19035
Acta Cryst. D 2001, 57, 745-747.

T. Knöfel and N. Sträter
E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion
J. Mol. Biol. 2001, 309, 255-266.

I. Przylas, Y. Terada, K. Fujii, T. Takaha, W. Saenger and N. Sträter
X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cycloamyloses
Eur. J. Biochem. 2000, 267, 6903-6913.

I. Przylas, K. Tomoo, Y. Terada, T. Takaha, S. Okada, W. Saenger and N. Sträter
Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalyzing the production of large cyclic glucans
J. Mol. Biol. 2000, 296, 873-886.

N. Sträter, D. J. Sherratt and S. D. Colloms
X-ray structure of aminopeptidase A from E. coli and a model for the nucleoprotein complex in Xer site-specific recombination
EMBO J. 1999, 18, 4513-4522.

T. Knöfel and N. Sträter
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
Nature Struct. Biol. 1999, 6, 448-453.

N. Sträter, L. Sun, E. R. Kantrowitz and W. N. Lipscomb
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase
Proc. Natl. Acad. Sci. USA 1999, 96, 11151-11155.

W. N. Lipscomb and N. Sträter
Yeast chorismate mutase and other allosteric enzymes
Pure & Appl. Chem. 1998, 70, 527-531.

N. Sträter and W. N. Lipscomb
Leucyl aminopeptidase (animal and plant)
in Handbook of proteolytic enzymes, pp. 1384-1389, Ed. A. J. Barrett, N. D. Rawlings, J. F. Woessner, Academic Press, New York, 1998.

N. Sträter, G. Schnappauf, G. H. Braus and W. N. Lipscomb
Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase by crystal structures
Structure 1997, 5, 1437-1452.

G. Schnappauf, N. Sträter, W. N. Lipscomb and G. H. Braus
A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions
Proc. Natl. Acad. Sci. USA 1997, 94, 8491-8496.

W. N. Lipscomb and N. Sträter
Recent advances in zinc enzymology
Chem. Rev. 1996, 96, 2375-2433.

N. Sträter, W. N. Lipscomb, T. Klabunde and B. Krebs
Two-metal ion catalysis in enzymatic acyl- and phosphoryl-transfer reactions
Chem. Int. Ed. Engl. 1996, 35, 2024-2055.

T. Klabunde, N. Sträter, R. Fröhlich, H. Witzel and B. Krebs
Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
J. Mol. Biol. 1996, 259, 737-748.

N. Sträter, K. Håkansson, G. Schnappauf, G. Braus and W. N. Lipscomb
Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state
Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 3330-3334.

N. Sträter and W. N. Lipscomb
Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography
Biochemistry 1995, 34, 14792-14800.

N. Sträter and W. N. Lipscomb
Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form
Biochemistry 1995, 34, 9200-9210.

N. Sträter and W. N. Lipscomb
Two-metal ion mechanism of leucine aminopeptidase. Binding of gem-diolate transition state analogues
J. Inorg. Biochem. 1995, 59, 294.

T. Klabunde, N. Sträter, B. Krebs and H. Witzel
Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases
FEBS Lett. 1995, 367, 56-60.

N. Sträter, T. Klabunde, P. Tucker, H. Witzel and B. Krebs
Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
Science 1995, 268, 1489-1492.

B. Krebs and N. Sträter
Highlights: X-ray structure analysis of methane monooxygenase: an important step toward understanding the oxidation of methane in biological systems
Chem. Int. Ed. Engl. 1994, 33, 841-843.

R. W. Berg, S. Boghosian, N. J. Bjerrum, R. Fehrmann, B. Krebs, N. Sträter, O. S. Mortensen and G. N. Papatheodorou
Crystal structure and spectroscopic characterization of CsV(SO
4)2. evidence for an electronic raman transition
Inorg. Chem. 1993, 32, 4714-4720.

N. Sträter, R. Fröhlich, A. Schiemann, B. Krebs, M. Körner, H. Suerbaum and H. Witzel Crystallization and preliminary crystallographic data of purple acid phosphatase from red kidney bean
J. Mol.
Biol. 1992, 224, 511-513.

R. Aumann, H. Heinen, P. Hinterding, N. Sträter and B. Krebs
1-Metalla-1,3,5-triene und 1-Metalla-1,3-dien-5-ine von Chrom und Wolfram, durch Insertion von Alkinen in M=C- bzw. C=C-Bindungen von 1-Metalla-1,3-dienen bzw. 1-Metalla-1-en-2-inen
Chem. Ber. 1991, 124, 1229-1236.