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Seminarthemen Kristallographiepraktikum 2015 mit Literaturvorschlägen
Validierung: Kleywegt, verschiedene Paper, z.B.
Acta Cryst D, 56 (2000), 249-265
Acta Cryst D, 65 (2009), 134-139
SAXS: Mertens, Svergun
J Struct Biol, 172 (2010), 128-141
Mertens, Svergun
FEBS J. 2014 Apr;281(8):1974-87. doi: 10.1111/febs.12772. Epub 2014 Mar 19.
Weak protein-ligand interactions studied by small-angle X-ray scattering.
Tuukkanen AT1, Svergun DI.
Methods. 2011 May;54(1):181-99. doi: 10.1016/j.ymeth.2011.01.004. Epub 2011 Jan 20.
Analytical ultracentrifugation combined with X-ray and neutron scattering: Experiment and modelling.
Perkins SJ1, Nan R, Li K, Khan S, Abe Y.
Protein Sci. 2014 Jun;23(6):669-82. doi: 10.1002/pro.2467. Epub 2014 Apr 17.
The dynamic duo: combining NMR and small angle scattering in structural biology.
Hennig J1, Sattler M.
Rigid body refinement and use in low resolution models, SAS
DESY, BioSAXS course 2012
Neutronenbeugung
Neutron crystallography: opportunities, challenges, and limitations.
Blakeley MP, Langan P, Niimura N, Podjarny A.
Curr Opin Struct Biol. 2008 Oct;18(5):593-600. doi: 10.1016/j.sbi.2008.06.009. Epub 2008 Aug 7. Review.
(Phasing von großen Komplexen mit Metallclustern bei niedriger Auflösung)
The phase problem:
Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1881-90. Epub 2003 Oct 23.
The phase problem.
Taylor G.
Data collection strategies:
Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1935-42. Epub 2003 Oct 23.
Optimizing data collection for structure determination.
González A.
Cryocooling, radiation damage, RIP:
Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):32-47. Epub 2005 Dec 14.
Cryocooling and radiation damage in macromolecular crystallography.
Garman EF, Owen RL.
MR:Acta Crystallographica Section D
Biological Crystallography
Acta Cryst. (2008) D64, 17–24
The befores and afters of molecular replacement
Eleanor Dodson
SAD/MAD using native proteins:
Science. 2012 May 25;336(6084):1033-7. doi: 10.1126/science.1218753.
Structures from anomalous diffraction of native biological macromolecules.
Liu Q, Dahmane T, Zhang Z, Assur Z, Brasch J, Shapiro L, Mancia F, Hendrickson WA.
Acta Crystallogr D Biol Crystallogr. 2013 Jul;69(Pt 7):1314-32. doi: 10.1107/S0907444913001479. Epub 2013 Jun 13.
Robust structural analysis of native biological macromolecules from multi-crystal anomalous diffraction data.
Liu Q, Liu Q, Hendrickson WA.
TLS:
Acta Crystallographica Section D
Biological Crystallography
Use of TLS parameters to model anisotropic displacements in macromolecular refinement
M. D.Winn, M. N. Isupov and G. N. Murshudov
Combining X-ray diffraction with other techniques (EM, NMR, fluorescence, ...):
FEBS J. 2013 Jan;280(1):28-45. doi: 10.1111/febs.12078. Epub 2012 Dec 17.
Cryo-electron microscopy--a primer for the non-microscopist.
Milne JL, Borgnia MJ, Bartesaghi A, Tran EE, Earl LA, Schauder DM, Lengyel J, Pierson J, Patwardhan A, Subramaniam S.
Curr Opin Struct Biol. 2008 Oct;18(5):617-22. doi: 10.1016/j.sbi.2008.07.004. Epub 2008 Sep 11.
United we stand: combining structural methods.
Cowieson NP, Kobe B, Martin JL.
Electron crystallography:
Methods Mol Biol. 2013;955:1-16. doi: 10.1007/978-1-62703-176-9_1.
Introduction to electron crystallography.
Kühlbrandt W.
nicht zugänglich
Curr Opin Struct Biol. 2012 Aug;22(4):514-9. doi: 10.1016/j.sbi.2012.03.006. Epub 2012 Apr 21.
Electron crystallography--the waking beauty of structural biology.
Pope CR, Unger VM.
Time-resolved crystallography:
Curr Opin Struct Biol. 2012 Oct;22(5):651-9. doi: 10.1016/j.sbi.2012.08.006. Epub 2012 Sep Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges.
Neutze R, Moffat K.
Time-resolved crystallography.
Moffat K.
Acta Crystallogr A. 1998 Nov 1;54(Pt 6 Pt 1):833-41. Review.
pH dependence of the photoactive yellow protein photocycle investigated by time-resolved crystallography.
Tripathi S, Srajer V, Purwar N, Henning R, Schmidt M.
Biophys J. 2012 Jan 18;102(2):325-32. doi: 10.1016/j.bpj.2011.11.4021.
Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser.
Kupitz C, Basu S, Grotjohann I, Fromme R, Zatsepin NA, Rendek KN, Hunter MS, Shoeman RL, White TA, Wang D, James D, Yang JH, Cobb DE, Reeder B, Sierra RG, Liu H, Barty A, Aquila AL, Deponte D, Kirian RA, Bari S, Bergkamp JJ, Beyerlein KR, Bogan MJ, Caleman C, Chao TC, Conrad CE, Davis KM, Fleckenstein H, Galli L, Hau-Riege SP, Kassemeyer S, Laksmono H, Liang M, Lomb L, Marchesini S, Martin AV, Messerschmidt M, Milathianaki D, Nass K, Ros A, Roy-Chowdhury S, Schmidt K, Seibert M, Steinbrener J, Stellato F, Yan L, Yoon C, Moore TA, Moore AL, Pushkar Y, Williams GJ, Boutet S, Doak RB, Weierstall U, Frank M, Chapman HN, Spence JC, Fromme P.
Nature. 2014 Sep 11;513(7517):261-5. doi: 10.1038/nature13453. Epub 2014 Jul 9.
Free-electron lasers:
Curr Opin Struct Biol. 2011 Aug;21(4):509-16. doi: 10.1016/j.sbi.2011.06.001.
Femtosecond nanocrystallography using X-ray lasers for membrane protein structure determination.
Fromme P, Spence JC.
Infra-red crystallography:
Biochim Biophys Acta. 2011 Jun;1814(6):760-77. doi: 10.1016/j.bbapap.2011.02.012. Epub 2011 Mar 2.
Infrared protein crystallography.
Sage JT, Zhang Y, McGeehan J, Ravelli RB, Weik M, van Thor JJ.
Microscale thermophoresis:
Bound or free: interaction of the C-terminal domain of Escherichia coli single-stranded DNA-binding protein (SSB) with the tetrameric core of SSB.
Su XC, Wang Y, Yagi H, Shishmarev D, Mason CE, Smith PJ, Vandevenne M, Dixon NE, Otting G.
Biochemistry. 2014 Apr 1;53(12):1925-34. doi: 10.1021/bi5001867. Epub 2014 Mar 18.
CD Spectroscopy:
Q Rev Biophys. 2009 Nov;42(4):317-70. doi: 10.1017/S003358351000003X.
Protein characterisation by synchrotron radiation circular dichroism spectroscopy.
Wallace BA.
Adv Protein Chem Struct Biol. 2010;80:85-115. doi: 10.1016/B978-0-12-381264-3.00003-5.
Mechanisms of protein circular dichroism: insights from computational modeling.
Karabencheva T, Christov C.
Biopolymers. 2008 May;89(5):392-400.
Protein secondary structure analyses from circular dichroism
spectroscopy: methods and reference databases. Whitmore L, Wallace BA.
MS:
Curr Opin Struct Biol. 2013 Apr;23(2):252-60. doi: 10.1016/j.sbi.2013.02.008. Epub 2013 Mar 20
Mass spectrometry supported determination of protein complex structure.
Walzthoeni T, Leitner A, Stengel F, Aebersold R.
Nat Chem. 2014 Apr;6(4):281-94. doi: 10.1038/nchem.1889.
The power of ion mobility-mass spectrometry for structural
characterization and the study of conformational dynamics. Lanucara F1,
Holman SW1, Gray CJ2, Eyers CE1.
J Struct Funct Genomics. 2013 Sep;14(3):77-90. doi: 10.1007/s10969-013-9160-z. Epub 2013 Aug 7.
Cross-linking and mass spectrometry methodologies to facilitate
structural biology: finding a path through the maze. Merkley ED1, Cort
JR, Adkins JN.
FEBS J. 2013 Nov;280(22):5616-25. doi: 10.1111/febs.12332. Epub 2013 Jun 11.
Characterizing rapid, activity-linked conformational transitions in
proteins via sub-second hydrogen deuterium exchange mass spectrometry.
Resetca D1, Wilson DJ.
Native ion mobility-mass spectrometry and related methods in structural biology.
Konijnenberg A, Butterer A, Sobott F.
Biochim Biophys Acta. 2013 Jun;1834(6):1239-56. doi:
10.1016/j.bbapap.2012.11.013. Epub 2012 Dec 14. Review.
Biochim Biophys Acta. 2013 Jun;1834(6):1188-201. doi: 10.1016/j.bbapap.2012.10.011. Epub 2012 Oct 29.
Biological insights from hydrogen exchange mass spectrometry.
Jaswal SS.
Thermostability:
Trends Biochem Sci. 2012 Sep;37(9):343-52. doi: 10.1016/j.tibs.2012.06.003. Epub 2012 Jul 10.
A crystal clear solution for determining G-protein-coupled receptor structures.
Tate CG.
A thermal stability assay can help to estimate the crystallization likelihood of biological samples.
Dupeux F, Röwer M, Seroul G, Blot D, Márquez JA. Acta Crystallogr D Biol
Crystallogr. 2011 Nov;67(Pt 11):915-9. doi: 10.1107/S0907444911036225. 2011
Phasing with low res models:
Acta Crystallogr D Biol Crystallogr. 2013 Nov;69(Pt 11):2257-65. doi: 10.1107/S0907444913022336. 2013
From lows to highs: using low-resolution models to phase X-ray data.
Stuart DI1, Abrescia NG.
Combined NMR/crystallography approaches:
In drug design:
Top Curr Chem. 2012;317:83-114. doi: 10.1007/128_2011_183.
Combining NMR and X-ray crystallography in fragment-based drug
discovery: discovery of highly potent and selective BACE-1 inhibitors.
Wyss DF1, Wang YS, Eaton HL, Strickland C, Voigt JH, Zhu Z, Stamford AW.
Electron microscopy:
J Struct Funct Genomics. 2014 Sep;15(3):117-24. doi: 10.1007/s10969-014-9179-9. 2014
Towards an integrative structural biology approach: combining Cryo-TEM,
X-ray crystallography, and NMR. Lengyel J1, Hnath E, Storms M, Wohlfarth
T.
Adv Protein Chem Struct Biol. 2011;82:1-35. doi: 10.1016/B978-0-12-386507-6.00001-4.
Atomic resolution cryo electron microscopy of macromolecular complexes.
Zhou ZH.
FRET:
Chemphyschem. 2011 Feb 25;12(3):542-53. doi: 10.1002/cphc.201000702. 2011
Improving FRET-based monitoring of single chemomechanical rotary motors at work.
Börsch M1, Wrachtrup J.
Unstructured proteins/NMR:
Proc Natl Acad Sci U S A. 2014 Aug 19;111(33):12079-84. doi: 10.1073/pnas.1402054111. 2014
Energetically significant networks of coupled interactions within an unfolded protein.
Cho JH1, Meng W2, Sato S2, Kim EY3, Schindelin H4, Raleigh DP5.
Integrative approaches:
Curr Opin Struct Biol. 2014 Sep 16;27C:138-148. doi: 10.1016/j.sbi.2014.08.006.
Function and dynamics of macromolecular complexes explored by
integrative structural and computational biology. Purdy MD1, Bennett
BC1, McIntire WE2, Khan AK1, Kasson PM3, Yeager M4.
Characterization of an Fe4S3 cluster:
Reversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenase.
Frielingsdorf S, Fritsch J, Schmidt A, Hammer M, Löwenstein J, Siebert E, Pelmenschikov V, Jaenicke T, Kalms J, Rippers Y, Lendzian F, Zebger I, Teutloff C, Kaupp M, Bittl R, Hildebrandt P, Friedrich B, Lenz O, Scheerer P.
Nat Chem Biol. 2014 May;10(5):378-85. doi: 10.1038/nchembio.1500. Epub 2014 Apr 6.
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre.
Fritsch J, Scheerer P, Frielingsdorf S, Kroschinsky S, Friedrich B, Lenz O, Spahn CM.
Nature. 2011 Oct 16;479(7372):249-52. doi: 10.1038/nature10505.
Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase.
Shomura Y, Yoon KS, Nishihara H, Higuchi Y.
Nature. 2011 Oct 16;479(7372):253-6. doi: 10.1038/nature10504.
EPR spectroscopic studies of the Fe-S clusters in the O2-tolerant [NiFe]-hydrogenase Hyd-1 from Escherichia coli and characterization of the unique [4Fe-3S] cluster by HYSCORE.
Roessler MM, Evans RM, Davies RA, Harmer J, Armstrong FA.
J Am Chem Soc. 2012 Sep 19;134(37):15581-94. Epub 2012 Sep 4. Erratum in: J Am Chem Soc. 2013 Mar 13;135(10):4159.
Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mossbauer and EPR spectroscopy.
Pandelia ME, Bykov D, Izsak R, Infossi P, Giudici-Orticoni MT, Bill E, Neese F, Lubitz W.
Proc Natl Acad Sci U S A. 2013 Jan 8;110(2):483-8. doi: 10.1073/pnas.1202575110. Epub 2012 Dec 24.
Redox-dependent structural transformations of the [4Fe-3S] proximal cluster in O2-tolerant membrane-bound [NiFe]-hydrogenase: a DFT study.
Pelmenschikov V, Kaupp M.
J Am Chem Soc. 2013 Aug 14;135(32):11809-23. doi: 10.1021/ja402159u. Epub 2013 Aug 5.
Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha.
J Am Chem Soc. 2014 Jun 18;136(24):8512-5. doi: 10.1021/ja503138p. Epub 2014 Jun 5.
Radu V1, Frielingsdorf S, Evans SD, Lenz O, Jeuken LJ.
Novel, oxygen-insensitive group 5 [NiFe]-hydrogenase in Ralstonia eutropha.
Schäfer C, Friedrich B, Lenz O.
Appl Environ Microbiol. 2013 Sep;79(17):5137-45. doi: 10.1128/AEM.01576-13. Epub 2013 Jun 21.
Detection of evolutionary relationships:
The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction.
Parthier C1, Görlich S, Jaenecke F, Breithaupt C, Bräuer U, Fandrich U, Clausnitzer D, Wehmeier UF, Böttcher C, Scheel D, Stubbs MT.
Angew Chem Int Ed Engl. 2012 Apr 23;51(17):4046-52. doi: 10.1002/anie.201108896. Epub 2012 Mar 1.
Crystallization with instable ligands:
A monovalent cation acts as structural and catalytic cofactor in translational GTPases.
Kuhle B1, Ficner R2
EMBO J. 2014 Sep 15. pii: e201488517. [Epub ahead of print]
Crystal structure of transglutaminase 2 with GTP complex and amino Acid sequence evidence of evolution of GTP binding site.
Jang TH, Lee DS, Choi K, Jeong EM, Kim IG, Kim YW, Chun JN, Jeon JH, Park HH.
PLoS One. 2014 Sep 5;9(9):e107005. doi: 10.1371/journal.pone.0107005. eCollection 2014.
Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide.
Zeraik AE1, Pereira HM, Santos YV, Brandão-Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araújo AP, DeMarco R.
J Biol Chem. 2014 Mar 14;289(11):7799-811. doi: 10.1074/jbc.M113.525352. Epub 2014 Jan 24.
Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis.
Luo L, Taylor KL, Xiang H, Wei Y, Zhang W, Dunaway-Mariano D.
Biochemistry. 2001 Dec 25;40(51):15684-92.
Design of metal binding sites:
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| Lerninhalte |
<p>Aktuelle Seminarthemen finden Sie im Moodle.</p><p>Seminarthemen Kristallographiepraktikum 2016 mit Literaturvorschlägen</p><p> </p><p>Die Vorträge sollen mehr methodisches als projektgebundenes erläutern. Meist steht also eine Methode im Labor oder am Rechner im Vordergrund. Die Physik oder der zugrundeliegende Vorgang werden erklärt und wie dies mit einem Gerät gemessen werden kann. Was kann mit der Methode gemessen oder erreicht werden, was sind die Vorteile, wo liegen die Nachteile. Ein Literaturbeispiel kann dies verdeutlichen.</p><p>Das Ziel ist nicht ein bestimmtes Paper wiederzugeben, sondern eine Methode zu vermitteln.</p><p><strong>X-ray crystallography, hardware and </strong><strong>methods</strong></p><p>Data collection strategies: Cryocooling, radiation damage, RIP: Electron crystallography: Time-resolved crystallography:</p><p>Free-electron lasers: Infra-red crystallography: Crystallization with instable ligands:</p><p><strong>X-ray crystallography, theory, structure solution and refinement</strong></p><p>Rigid body refinement and use in low resolution models, SAS</p><p>(Phasing von großen Komplexen mit Metallclustern bei niedriger Auflösung)</p><p>The phase problem: MR: Acta Crystallographica Section D SAD/MAD using native proteins: TLS: Phasing with low res models: <strong>Other diffraction methods</strong></p><p>Neutronenbeugung</p><p>Electron microscopy: <strong>Biophysical methods</strong></p><p>SAXS: Mertens, Svergun</p><p>FRET: Combining X-ray diffraction with other techniques (EM, NMR, fluorescence, ...): Combined NMR/crystallography approaches: Integrative approaches: Microscale thermophoresis:</p><p>CD Spectroscopy: MS: Thermostability: Unstructured proteins/NMR: <strong>Structure analysis</strong></p><p>Validierung: Kleywegt, verschiedene Paper, z.B.</p><p>Characterization of an Fe<sub>4</sub>S<sub>3</sub> cluster:</p><p>Detection of evolutionary relationships:</p><p>Design of metal binding sites:</p><p><strong> </strong></p><p><strong> </strong></p><p><strong>Validierung: Kleywegt, verschiedene Paper, z.B.</strong></p><p> </p><p>Acta Cryst D, 56 (2000), 249-265</p><p>Acta Cryst D, 65 (2009), 134-139</p><p> </p><p><strong>SAXS: Mertens, Svergun</strong></p><p> </p><p>J Struct Biol, 172 (2010), 128-141</p><p>Mertens, Svergun</p><p>FEBS J. 2014 Apr;281(8):1974-87. doi: 10.1111/febs.12772. Epub 2014 Mar 19. Weak protein-ligand interactions studied by small-angle X-ray scattering. Tuukkanen AT1, Svergun DI. Methods. 2011 May;54(1):181-99. doi: 10.1016/j.ymeth.2011.01.004. Epub 2011 Jan 20. Analytical ultracentrifugation combined with X-ray and neutron scattering: Experiment and modelling. Perkins SJ1, Nan R, Li K, Khan S, Abe Y. Protein Sci. 2014 Jun;23(6):669-82. doi: 10.1002/pro.2467. Epub 2014 Apr 17. The dynamic duo: combining NMR and small angle scattering in structural biology. Hennig J1, Sattler M. <strong>Rigid body refinement and use in low resolution models, SAS</strong></p><p> </p><p>DESY, BioSAXS course 2012</p><p> </p><p><strong>Neutronenbeugung</strong></p><p> </p><p>Neutron crystallography: opportunities, challenges, and limitations.</p><p>Blakeley MP, Langan P, Niimura N, Podjarny A.</p><p>Curr Opin Struct Biol. 2008 Oct;18(5):593-600. doi: 10.1016/j.sbi.2008.06.009. Epub 2008 Aug 7. Review.</p><p> </p><p><strong>(Phasing von großen Komplexen mit Metallclustern bei niedriger Auflösung)</strong></p><p> </p><p><strong>The phase problem: </strong> Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1881-90. Epub 2003 Oct 23. The phase problem. Taylor G. <strong>Data collection strategies: </strong></p><p>Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1935-42. Epub 2003 Oct 23. Optimizing data collection for structure determination. González A. <strong>Cryocooling, radiation damage, RIP:</strong></p><p>Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):32-47. Epub 2005 Dec 14. Cryocooling and radiation damage in macromolecular crystallography. Garman EF, Owen RL. <strong>MR: </strong>Acta Crystallographica Section D Biological Crystallography Acta Cryst. (2008) D64, 17–24 The befores and afters of molecular replacement Eleanor Dodson <strong>SAD/MAD using native proteins: </strong></p><ol start="7"><li>Structures from anomalous diffraction of native biological macromolecules. Liu Q, Dahmane T, Zhang Z, Assur Z, Brasch J, Shapiro L, Mancia F, Hendrickson WA. Acta Crystallogr D Biol Crystallogr. 2013 Jul;69(Pt 7):1314-32. doi: 10.1107/S0907444913001479. Epub 2013 Jun 13. Robust structural analysis of native biological macromolecules from multi-crystal anomalous diffraction data. Liu Q, Liu Q, Hendrickson WA. <strong>TLS: </strong></li></ol><p>Acta Crystallographica Section D Biological Crystallography Use of TLS parameters to model anisotropic displacements in macromolecular refinement M. D.Winn, M. N. Isupov and G. N. Murshudov <strong>Combining X-ray diffraction with other techniques (EM, NMR, fluorescence, ...): </strong></p><p>FEBS J. 2013 Jan;280(1):28-45. doi: 10.1111/febs.12078. Epub 2012 Dec 17. Cryo-electron microscopy--a primer for the non-microscopist. Milne JL, Borgnia MJ, Bartesaghi A, Tran EE, Earl LA, Schauder DM, Lengyel J, Pierson J, Patwardhan A, Subramaniam S. Curr Opin Struct Biol. 2008 Oct;18(5):617-22. doi: 10.1016/j.sbi.2008.07.004. Epub 2008 Sep 11. United we stand: combining structural methods. Cowieson NP, Kobe B, Martin JL. <strong>Electron crystallography: </strong> Methods Mol Biol. 2013;955:1-16. doi: 10.1007/978-1-62703-176-9_1. Introduction to electron crystallography. Kühlbrandt W. nicht zugänglich</p><p>Curr Opin Struct Biol. 2012 Aug;22(4):514-9. doi: 10.1016/j.sbi.2012.03.006. Epub 2012 Apr 21. Electron crystallography--the waking beauty of structural biology. Pope CR, Unger VM. <strong>Time-resolved crystallography: </strong> Curr Opin Struct Biol. 2012 Oct;22(5):651-9. doi: 10.1016/j.sbi.2012.08.006. Epub 2012 Sep Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges. Neutze R, Moffat K. <a href="http://www.ncbi.nlm.nih.gov/pubmed/9859195">Time-resolved crystallography.</a></p><p>Moffat K.</p><p>Acta Crystallogr A. 1998 Nov 1;54(Pt 6 Pt 1):833-41. Review.</p><p> </p><p><a href="http://www.ncbi.nlm.nih.gov/pubmed/22339869">pH dependence of the photoactive yellow protein photocycle investigated by time-resolved crystallography.</a></p><p>Tripathi S, Srajer V, Purwar N, Henning R, Schmidt M.</p><p>Biophys J. 2012 Jan 18;102(2):325-32. doi: 10.1016/j.bpj.2011.11.4021.</p><p> </p><p><a href="http://www.ncbi.nlm.nih.gov/pubmed/25043005">Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser.</a></p><p>Kupitz C, Basu S, Grotjohann I, Fromme R, Zatsepin NA, Rendek KN, Hunter MS, Shoeman RL, White TA, Wang D, James D, Yang JH, Cobb DE, Reeder B, Sierra RG, Liu H, Barty A, Aquila AL, Deponte D, Kirian RA, Bari S, Bergkamp JJ, Beyerlein KR, Bogan MJ, Caleman C, Chao TC, Conrad CE, Davis KM, Fleckenstein H, Galli L, Hau-Riege SP, Kassemeyer S, Laksmono H, Liang M, Lomb L, Marchesini S, Martin AV, Messerschmidt M, Milathianaki D, Nass K, Ros A, Roy-Chowdhury S, Schmidt K, Seibert M, Steinbrener J, Stellato F, Yan L, Yoon C, Moore TA, Moore AL, Pushkar Y, Williams GJ, Boutet S, Doak RB, Weierstall U, Frank M, Chapman HN, Spence JC, Fromme P.</p><p>Nature. 2014 Sep 11;513(7517):261-5. doi: 10.1038/nature13453. Epub 2014 Jul 9.</p><p><strong>Free-electron lasers: </strong> Curr Opin Struct Biol. 2011 Aug;21(4):509-16. doi: 10.1016/j.sbi.2011.06.001. Femtosecond nanocrystallography using X-ray lasers for membrane protein structure determination. Fromme P, Spence JC. <strong>Infra-red crystallography: </strong> Biochim Biophys Acta. 2011 Jun;1814(6):760-77. doi: 10.1016/j.bbapap.2011.02.012. Epub 2011 Mar 2. Infrared protein crystallography. Sage JT, Zhang Y, McGeehan J, Ravelli RB, Weik M, van Thor JJ.</p><p><strong>Microscale thermophoresis: </strong></p><p> </p><p><a href="http://www.ncbi.nlm.nih.gov/pubmed/24606314">Bound or free: interaction of the C-terminal domain of Escherichia coli single-stranded DNA-binding protein (SSB) with the tetrameric core of SSB.</a></p><p>Su XC, Wang Y, Yagi H, Shishmarev D, Mason CE, Smith PJ, Vandevenne M, Dixon NE, Otting G.</p><p>Biochemistry. 2014 Apr 1;53(12):1925-34. doi: 10.1021/bi5001867. Epub 2014 Mar 18.</p><p> </p><p><strong>CD Spectroscopy</strong>:</p><p>Q Rev Biophys. 2009 Nov;42(4):317-70. doi: 10.1017/S003358351000003X. Protein characterisation by synchrotron radiation circular dichroism spectroscopy. Wallace BA. Adv Protein Chem Struct Biol. 2010;80:85-115. doi: 10.1016/B978-0-12-381264-3.00003-5. Mechanisms of protein circular dichroism: insights from computational modeling. Karabencheva T, Christov C. Biopolymers. 2008 May;89(5):392-400. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Whitmore L, Wallace BA. <strong>MS: </strong> Curr Opin Struct Biol. 2013 Apr;23(2):252-60. doi: 10.1016/j.sbi.2013.02.008. Epub 2013 Mar 20 Mass spectrometry supported determination of protein complex structure. Walzthoeni T, Leitner A, Stengel F, Aebersold R. Nat Chem. 2014 Apr;6(4):281-94. doi: 10.1038/nchem.1889. 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