메뉴 건너뛰기




Volumn 13, Issue 3, 2012, Pages 3782-3800

Increasing the X-ray diffraction power of protein crystals by dehydration: The case of bovine serum albumin and a survey of literature data

Author keywords

Crystal dehydration; Crystal quality; Post crystallization treatment; Protein crystallization; Serum albumin; X ray crystallography

Indexed keywords

APOLIPOPROTEIN A4; BOVINE SERUM ALBUMIN; CYTOCHROME C OXIDASE; DIPEPTIDYL PEPTIDASE; FATTY ACID; FATTY ACID SYNTHASE; FATTY ACID TRANSPORTER; FERREDOXIN; FERREDOXIN REDUCTASE; GLUTARYL 7 AMINOCEPHALOSPORANIC ACID ACYLASE; HEMIN; HUMAN SERUM ALBUMIN; LIPASE FOLDASE COMPLEX; LOCAL ANESTHETIC AGENT; MAOC LIKE DEHYDRATASE; MONOCLINIC LYSOZYME; N ACETYLGLUCOSAMINE 1 PHOSPHATE URIDYLTRANSFERASE; NECTIN 1 EC COMPLEX; PENICILLIN AMIDASE; PEPTIDE DEFORMYLASE; PHOSPHOGLYCERATE KINASE; PLASMA PROTEIN; PORPHOBILINOGEN SYNTHASE; PROTEIN; PYRUVATE DEHYDROGENASE; STAT1 PROTEIN; TETRAGONAL LYSOZYME; THIOREDOXIN; TREHALOSE PHOSPHORYLASE; TRICOM INTERACTING FACTOR F3; UNCLASSIFIED DRUG;

EID: 84858964808     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13033782     Document Type: Article
Times cited : (44)

References (96)
  • 1
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D.C.; Ho, J.X. Structure of serum albumin. Adv. Protein Chem. 1994, 45, 153-203.
    • (1994) Adv. Protein Chem , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 3
    • 0025913301 scopus 로고
    • The role of serum proteins in acid-base equilibria
    • Figge, J.; Rossing, T.H.; Fencl, V. The role of serum proteins in acid-base equilibria. J. Lab. Clin. Med. 1991, 117, 453-467.
    • (1991) J. Lab. Clin. Med , vol.117 , pp. 453-467
    • Figge, J.1    Rossing, T.H.2    Fencl, V.3
  • 4
    • 0018596292 scopus 로고
    • Binding of drugs to human serum albumin:XI. The specificity of three binding sites as studied with albumin immobilized in microparticles
    • Sjoholm, I.; Ekman, B.; Kober, A.; Ljungstedt-Pahlman, I.; Seiving, B.; Sjodin, T. Binding of drugs to human serum albumin:XI. The specificity of three binding sites as studied with albumin immobilized in microparticles. Mol. Pharmacol. 1979, 16, 767-777.
    • (1979) Mol. Pharmacol , vol.16 , pp. 767-777
    • Sjoholm, I.1    Ekman, B.2    Kober, A.3    Ljungstedt-Pahlman, I.4    Seiving, B.5    Sjodin, T.6
  • 5
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X.M.; Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature 1992, 358, 209-215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 6
    • 65249172433 scopus 로고    scopus 로고
    • Physicochemical and conformational studies on BSA-surfactant interaction in aqueous medium
    • Chakraborty, T.; Chakraborty, I.; Moulik, S.P.; Ghosh, S. Physicochemical and conformational studies on BSA-surfactant interaction in aqueous medium. Langmuir 2009, 25, 3062-3074.
    • (2009) Langmuir , vol.25 , pp. 3062-3074
    • Chakraborty, T.1    Chakraborty, I.2    Moulik, S.P.3    Ghosh, S.4
  • 7
    • 49449116404 scopus 로고    scopus 로고
    • Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes
    • Abou-Zied, O.K.; Al-Shihi, O.I. Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes. J. Am. Chem. Soc. 2008, 130, 10793-10801.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 10793-10801
    • Abou-Zied, O.K.1    Al-Shihi, O.I.2
  • 8
    • 0027417602 scopus 로고
    • PH-induced structural transitions of bovine serum albumin. Histidine pKa values and unfolding of the N-terminus during the N to F transition
    • Sadler, P.J.; Tucker, A. PH-induced structural transitions of bovine serum albumin. Histidine pKa values and unfolding of the N-terminus during the N to F transition. Eur. J. Biochem. 1993, 212, 811-817.
    • (1993) Eur. J. Biochem , vol.212 , pp. 811-817
    • Sadler, P.J.1    Tucker, A.2
  • 10
    • 4344588993 scopus 로고
    • New type of x-ray evidence on the molecular structure of globular proteins
    • Riley, D.P.; Arndt, U.W. New type of x-ray evidence on the molecular structure of globular proteins. Nature 1952, 169, 138-139.
    • (1952) Nature , vol.169 , pp. 138-139
    • Riley, D.P.1    Arndt, U.W.2
  • 11
    • 0040294884 scopus 로고
    • The effect of electric charge on the diffusion of macromolecules
    • Doherty, P.; Benedek, G.B. The effect of electric charge on the diffusion of macromolecules. J. Chem. Phys. 1974, 61, 5426-5435.
    • (1974) J. Chem. Phys , vol.61 , pp. 5426-5435
    • Doherty, P.1    Benedek, G.B.2
  • 12
    • 0039407231 scopus 로고
    • Neurath, H., Biley, K., Eds.; Academic Press: New York, NY, USA
    • Hughes, W.L. The Proteins; Neurath, H., Biley, K., Eds.; Academic Press: New York, NY, USA, 1954; Volume 2b, pp. 663-755.
    • (1954) The Proteins , vol.2 b , pp. 663-755
    • Hughes, W.L.1
  • 13
    • 0001176605 scopus 로고
    • Structure and interparticle interactions of bovine serum albumin in solution studied by small-angle neutron scattering
    • Bendedouch, D.; Chen, S.H. Structure and interparticle interactions of bovine serum albumin in solution studied by small-angle neutron scattering. J. Phys. Chem. 1983, 87, 1473-1477.
    • (1983) J. Phys. Chem , vol.87 , pp. 1473-1477
    • Bendedouch, D.1    Chen, S.H.2
  • 14
    • 0024548387 scopus 로고
    • The molecular mechanism of the neutral-to-base transition of human serum albumin. Acid/base titration and proton nuclear magnetic resonance studies on a large peptic and a large tryptic fragment of albumin
    • Bos, O.J.; Labro, J.F.; Fischer, M.J.; Wilting, J.; Janssen, L.H. The molecular mechanism of the neutral-to-base transition of human serum albumin. Acid/base titration and proton nuclear magnetic resonance studies on a large peptic and a large tryptic fragment of albumin. J. Biol. Chem. 1989, 264, 953-959.
    • (1989) J. Biol. Chem , vol.264 , pp. 953-959
    • Bos, O.J.1    Labro, J.F.2    Fischer, M.J.3    Wilting, J.4    Janssen, L.H.5
  • 17
    • 0031407808 scopus 로고    scopus 로고
    • Interfacial aggregation of bovine serum albumin related to crystallization conditions studied by total internal reflection fluorescence
    • Asanov, A.N.; Delucas, L.J.; Oldham, P.B.; Wilson, W.W. Interfacial aggregation of bovine serum albumin related to crystallization conditions studied by total internal reflection fluorescence. J. Colloid Interface Sci. 1997, 196, 62-73.
    • (1997) J. Colloid Interface Sci , vol.196 , pp. 62-73
    • Asanov, A.N.1    Delucas, L.J.2    Oldham, P.B.3    Wilson, W.W.4
  • 18
    • 32944467057 scopus 로고    scopus 로고
    • Post-crystallization treatments for improving diffraction quality of protein crystals
    • Heras, B.; Martin, J.L. Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallogr. D Biol. Crystallogr. 2005, 61, 1173-1180.
    • (2005) Acta Crystallogr. D Biol. Crystallogr , vol.61 , pp. 1173-1180
    • Heras, B.1    Martin, J.L.2
  • 19
    • 33644878456 scopus 로고    scopus 로고
    • A review of techniques for maximizing diffraction from a protein crystal in stilla
    • Newman, J. A review of techniques for maximizing diffraction from a protein crystal in stilla. Acta Crystallogr. D Biol. Crystallogr. 2006, 62, 27-31.
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 27-31
    • Newman, J.1
  • 20
    • 80053206933 scopus 로고    scopus 로고
    • Improving protein crystal quality by the without-oil microbatch method: Crystallization and preliminary x-ray diffraction analysis of glutathione synthetase from pseudoalteromonas haloplanktis
    • Merlino, A.; Russo Krauss, I.; Albino, A.; Pica, A.; Vergara, A.; Masullo, M.; De Vendittis, E.; Sica, F. Improving protein crystal quality by the without-oil microbatch method: Crystallization and preliminary x-ray diffraction analysis of glutathione synthetase from pseudoalteromonas haloplanktis. Int. J. Mol. Sci. 2011, 12, 6312-6319.
    • (2011) Int. J. Mol. Sci , vol.12 , pp. 6312-6319
    • Merlino, A.1    Russo, K.I.2    Albino, A.3    Pica, A.4    Vergara, A.5    Masullo, M.6    de Vendittis, E.7    Sica, F.8
  • 21
    • 0032127946 scopus 로고    scopus 로고
    • Macromolecular crystal annealing: Overcoming increased mosaicity associated with cryocrystallography
    • arp, J.M.; Timm, D.E.; Bunick, G.J. Macromolecular crystal annealing: Overcoming increased mosaicity associated with cryocrystallography. Acta Crystallogr. D Biol. Crystallogr. 1998, 54, 622-628.
    • (1998) Acta Crystallogr. D Biol. Crystallogr , vol.54 , pp. 622-628
    • Arp, J.M.1    Timm, D.E.2    Bunick, G.J.3
  • 24
    • 0037318396 scopus 로고    scopus 로고
    • Dehydration converts DsbG crystal diffraction from low to high resolution
    • Heras, B.; Edeling, M.A.; Byriel, K.A.; Jones, A.; Raina, S.; Martin, J.L. Dehydration converts DsbG crystal diffraction from low to high resolution. Structure 2003, 11, 139-145.
    • (2003) Structure , vol.11 , pp. 139-145
    • Heras, B.1    Edeling, M.A.2    Byriel, K.A.3    Jones, A.4    Raina, S.5    Martin, J.L.6
  • 25
    • 16644391685 scopus 로고    scopus 로고
    • Spectacular improvement of X-ray diffraction through fast desiccation of protein crystals
    • Abergel, C. Spectacular improvement of X-ray diffraction through fast desiccation of protein crystals. Acta Crystallogr. D Biol. Crystallogr. 2004, 60, 1413-1416.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 1413-1416
    • Abergel, C.1
  • 28
    • 0035997155 scopus 로고    scopus 로고
    • Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae
    • Pang, S.S.; Guddat, L.W.; Duggleby, R.G. Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 1237-1239.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1237-1239
    • Pang, S.S.1    Guddat, L.W.2    Duggleby, R.G.3
  • 30
    • 9344241404 scopus 로고    scopus 로고
    • Structure of human brain fructose 1,6-(bis)phosphate aldolase: Linking isozyme structure with function
    • Arakaki, T.L.; Pezza, J.A.; Cronin, M.A.; Hopkins, C.E.; Zimmer, D.B.; Tolan, D.R.; Allen, K.N. Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function. Protein Sci. 2004, 13, 3077-3084.
    • (2004) Protein Sci , vol.13 , pp. 3077-3084
    • Arakaki, T.L.1    Pezza, J.A.2    Cronin, M.A.3    Hopkins, C.E.4    Zimmer, D.B.5    Tolan, D.R.6    Allen, K.N.7
  • 31
    • 14144250670 scopus 로고    scopus 로고
    • Structure of the thermolabile mutant aldolase B, A149P: Molecular basis of hereditary fructose intolerance
    • Malay, A.D.; Allen, K.N.; Tolan, D.R. Structure of the thermolabile mutant aldolase B, A149P: Molecular basis of hereditary fructose intolerance. J. Mol. Biol. 2005, 347, 135-144.
    • (2005) J. Mol. Biol , vol.347 , pp. 135-144
    • Malay, A.D.1    Allen, K.N.2    Tolan, D.R.3
  • 32
    • 33745057880 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase
    • Igura, M.; Ose, T.; Obita, T.; Sato, C.; Maenaka, K.; Endo, T.; Kohda, D. Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2005, 61, 514-517.
    • (2005) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.61 , pp. 514-517
    • Igura, M.1    Ose, T.2    Obita, T.3    Sato, C.4    Maenaka, K.5    Endo, T.6    Kohda, D.7
  • 33
    • 67649097182 scopus 로고    scopus 로고
    • Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation
    • Bailly, M.; Blaise, M.; Lorber, B.; Thirup, S.; Kern, D. Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2009, 65, 577-581.
    • (2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.65 , pp. 577-581
    • Bailly, M.1    Blaise, M.2    Lorber, B.3    Thirup, S.4    Kern, D.5
  • 36
    • 0035782685 scopus 로고    scopus 로고
    • Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD
    • Haebel, P.W.; Wichman, S.; Goldstone, D.; Metcalf, P. Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD. J. Struct. Biol. 2001, 136, 162-166.
    • (2001) J. Struct. Biol , vol.136 , pp. 162-166
    • Haebel, P.W.1    Wichman, S.2    Goldstone, D.3    Metcalf, P.4
  • 37
    • 0030898068 scopus 로고    scopus 로고
    • Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals
    • Izard, T.; Sarfaty, S.; Westphal, A.; de Kok, A.; Hol, W.G. Improvement of diffraction quality upon rehydration of dehydrated icosahedral Enterococcus faecalis pyruvate dehydrogenase core crystals. Protein Sci. 1997, 6, 913-915.
    • (1997) Protein Sci , vol.6 , pp. 913-915
    • Izard, T.1    Sarfaty, S.2    Westphal, A.3    de Kok, A.4    Hol, W.G.5
  • 38
    • 0036177544 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a beta-ketoacyl carrier protein reductase homologue
    • Yang, J.K.; Yoon, H.J.; Ahn, H.J.; Lee, B.I.; Cho, S.H.; Waldo, G.S.; Park, M.S.; Suh, S.W. Crystallization and preliminary X-ray crystallographic analysis of the Rv2002 gene product from Mycobacterium tuberculosis, a beta-ketoacyl carrier protein reductase homologue. Acta Crystallogr. D Biol. Crystallogr. 2002, 58, 303-305.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 303-305
    • Yang, J.K.1    Yoon, H.J.2    Ahn, H.J.3    Lee, B.I.4    Cho, S.H.5    Waldo, G.S.6    Park, M.S.7    Suh, S.W.8
  • 40
    • 0037292373 scopus 로고    scopus 로고
    • Increasing the diffraction limit and internal order of a membrane protein crystal by dehydration
    • Kuo, A.; Bowler, M.W.; Zimmer, J.; Antcliff, J.F.; Doyle, D.A. Increasing the diffraction limit and internal order of a membrane protein crystal by dehydration. J. Struct. Biol. 2003, 141, 97-102.
    • (2003) J. Struct. Biol , vol.141 , pp. 97-102
    • Kuo, A.1    Bowler, M.W.2    Zimmer, J.3    Antcliff, J.F.4    Doyle, D.A.5
  • 41
    • 24044442616 scopus 로고    scopus 로고
    • A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus
    • Hunsicker-Wang, L.M.; Pacoma, R.L.; Chen, Y.; Fee, J.A.; Stout, C.D. A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus. Acta Crystallogr. D Biol. Crystallogr. 2005, 61, 340-343.
    • (2005) Acta Crystallogr. D Biol. Crystallogr , vol.61 , pp. 340-343
    • Hunsicker-Wang, L.M.1    Pacoma, R.L.2    Chen, Y.3    Fee, J.A.4    Stout, C.D.5
  • 42
    • 77956526892 scopus 로고    scopus 로고
    • Cloning, expression, purification, crystallization and preliminary crystallographic analysis of 5-aminolaevulinic acid dehydratase from Bacillus subtilis
    • Lu, Q.; Ma, J.; Rong, H.; Fan, J.; Yuan, Y.; Li, K.; Gao, Y.; Zhang, X.; Teng, M.; Niu, L. Cloning, expression, purification, crystallization and preliminary crystallographic analysis of 5-aminolaevulinic acid dehydratase from Bacillus subtilis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2010, 66, 1053-1055.
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.66 , pp. 1053-1055
    • Lu, Q.1    Ma, J.2    Rong, H.3    Fan, J.4    Yuan, Y.5    Li, K.6    Gao, Y.7    Zhang, X.8    Teng, M.9    Niu, L.10
  • 43
    • 2442563409 scopus 로고    scopus 로고
    • Crystal structure of protoporphyrinogen IX oxidase: A key enzyme in haem and chlorophyll biosynthesis
    • Koch, M.; Breithaupt, C.; Kiefersauer, R.; Freigang, J.; Huber, R.; Messerschmidt, A. Crystal structure of protoporphyrinogen IX oxidase: A key enzyme in haem and chlorophyll biosynthesis. EMBO J. 2004, 23, 1720-1728.
    • (2004) EMBO J , vol.23 , pp. 1720-1728
    • Koch, M.1    Breithaupt, C.2    Kiefersauer, R.3    Freigang, J.4    Huber, R.5    Messerschmidt, A.6
  • 44
    • 33748358154 scopus 로고    scopus 로고
    • Reproducible improvements in order and diffraction limit of crystals of bovine mitochondrial F(1)-ATPase by controlled dehydration
    • Bowler, M.W.; Montgomery, M.G.; Leslie, A.G.; Walker, J.E. Reproducible improvements in order and diffraction limit of crystals of bovine mitochondrial F(1)-ATPase by controlled dehydration. Acta Crystallogr. D Biol. Crystallogr. 2006, 62, 991-995.
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 991-995
    • Bowler, M.W.1    Montgomery, M.G.2    Leslie, A.G.3    Walker, J.E.4
  • 47
    • 19544377390 scopus 로고    scopus 로고
    • Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations
    • Kyrieleis, O.J.; Goettig, P.; Kiefersauer, R.; Huber, R.; Brandstetter, H. Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations. J. Mol. Biol. 2005, 349, 787-800.
    • (2005) J. Mol. Biol , vol.349 , pp. 787-800
    • Kyrieleis, O.J.1    Goettig, P.2    Kiefersauer, R.3    Huber, R.4    Brandstetter, H.5
  • 49
    • 4344596976 scopus 로고    scopus 로고
    • Crystallization of RNA and RNA-protein complexes
    • Ke, A.; Doudna, J.A. Crystallization of RNA and RNA-protein complexes. Methods 2004, 34, 408-414.
    • (2004) Methods , vol.34 , pp. 408-414
    • Ke, A.1    Doudna, J.A.2
  • 50
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman, G.D.; O'Donnell, M.; Kuriyan, J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 2004, 429, 724-730.
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 51
    • 83055165596 scopus 로고    scopus 로고
    • Improved X-ray diffraction from Bacillus megaterium penicillin G acylase crystals through long cryosoaking dehydration
    • Rojviriya, C.; Pratumrat, T.; Saper, M.A.; Yuvaniyama, J. Improved X-ray diffraction from Bacillus megaterium penicillin G acylase crystals through long cryosoaking dehydration. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2011, 67, 1570-1574.
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.67 , pp. 1570-1574
    • Rojviriya, C.1    Pratumrat, T.2    Saper, M.A.3    Yuvaniyama, J.4
  • 52
    • 36849035454 scopus 로고    scopus 로고
    • An unexpected outcome of surface engineering an integral membrane protein: Improved crystallization of cytochrome ba(3) from Thermus thermophilus
    • Liu, B.; Luna, V.M.; Chen, Y.; Stout, C.D.; Fee, J.A. An unexpected outcome of surface engineering an integral membrane protein: Improved crystallization of cytochrome ba(3) from Thermus thermophilus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2007, 63, 1029-1034.
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.63 , pp. 1029-1034
    • Liu, B.1    Luna, V.M.2    Chen, Y.3    Stout, C.D.4    Fee, J.A.5
  • 54
    • 34247576821 scopus 로고    scopus 로고
    • The structure of a plant photosystem I supercomplex at 3.4 A resolution
    • Amunts, A.; Drory, O.; Nelson, N. The structure of a plant photosystem I supercomplex at 3.4 A resolution. Nature 2007, 447, 58-63.
    • (2007) Nature , vol.447 , pp. 58-63
    • Amunts, A.1    Drory, O.2    Nelson, N.3
  • 59
    • 79955081730 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of recombinant chlorocatechol 1,2-dioxygenase from Pseudomonas putida
    • Rustiguel, J.K.; Pinheiro, M.P.; Araujo, A.P.; Nonato, M.C. Crystallization and preliminary X-ray diffraction analysis of recombinant chlorocatechol 1,2-dioxygenase from Pseudomonas putida. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2011, 67, 507-509.
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.67 , pp. 507-509
    • Rustiguel, J.K.1    Pinheiro, M.P.2    Araujo, A.P.3    Nonato, M.C.4
  • 63
    • 77953157168 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray analysis of the EIICGlc domain of the Escherichia coli glucose transporter
    • Zurbriggen, A.; Schneider, P.; Bahler, P.; Baumann, U.; Erni, B. Expression, purification, crystallization and preliminary X-ray analysis of the EIICGlc domain of the Escherichia coli glucose transporter. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2010, 66, 684-688.
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.66 , pp. 684-688
    • Zurbriggen, A.1    Schneider, P.2    Bahler, P.3    Baumann, U.4    Erni, B.5
  • 64
    • 77749301315 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the MaoC-like dehydratase from Phytophthora capsici
    • Wang, H.; Guo, J.; Pang, H.; Zhang, X. Crystallization and preliminary X-ray analysis of the MaoC-like dehydratase from Phytophthora capsici. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2010, 66, 272-274.
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.66 , pp. 272-274
    • Wang, H.1    Guo, J.2    Pang, H.3    Zhang, X.4
  • 65
    • 58849092366 scopus 로고    scopus 로고
    • Imperfect pseudo-merohedral twinning in crystals of fungal fatty acid synthase
    • Jenni, S.; Ban, N. Imperfect pseudo-merohedral twinning in crystals of fungal fatty acid synthase. Acta Crystallogr. D Biol. Crystallogr. 2009, 65, 101-111.
    • (2009) Acta Crystallogr. D Biol. Crystallogr , vol.65 , pp. 101-111
    • Jenni, S.1    Ban, N.2
  • 66
    • 40449112281 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analyses of Nur, a nickel-responsive transcription regulator from Streptomyces coelicolor
    • An, Y.J.; Ahn, B.E.; Roe, J.H.; Cha, S.S. Crystallization and preliminary X-ray crystallographic analyses of Nur, a nickel-responsive transcription regulator from Streptomyces coelicolor. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2008, 64, 130-132.
    • (2008) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.64 , pp. 130-132
    • An, Y.J.1    Ahn, B.E.2    Roe, J.H.3    Cha, S.S.4
  • 67
    • 34548303848 scopus 로고    scopus 로고
    • Effect of a sodium ion on the dehydration-induced phase transition of monoclinic lysozyme crystals
    • Harata, K.; Akiba, T. Effect of a sodium ion on the dehydration-induced phase transition of monoclinic lysozyme crystals. Acta Crystallogr. D Biol. Crystallogr. 2007, 63, 1016-1021.
    • (2007) Acta Crystallogr. D Biol. Crystallogr , vol.63 , pp. 1016-1021
    • Harata, K.1    Akiba, T.2
  • 68
    • 34249734768 scopus 로고    scopus 로고
    • Expression and purification of F-plasmid RepE and preliminary X-ray crystallographic study of its complex with operator DNA
    • Nakamura, A.; Wada, C.; Miki, K. Expression and purification of F-plasmid RepE and preliminary X-ray crystallographic study of its complex with operator DNA. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2007, 63, 346-349.
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.63 , pp. 346-349
    • Nakamura, A.1    Wada, C.2    Miki, K.3
  • 69
    • 34248212994 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009
    • Peng, Y.; Xu, F.; Bell, S.G.; Wong, L.L.; Rao, Z. Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2007, 63, 422-425.
    • (2007) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.63 , pp. 422-425
    • Peng, Y.1    Xu, F.2    Bell, S.G.3    Wong, L.L.4    Rao, Z.5
  • 73
    • 0001308823 scopus 로고
    • Protein hydration and water structure: X-ray analysis of a closely packed protein crystal with very low solvent content
    • Madhusudan; Kodandapani, R.; Vijayan, M. Protein hydration and water structure: X-ray analysis of a closely packed protein crystal with very low solvent content. Acta Crystallogr. D Biol. Crystallogr. 1993, 49, 234-245.
    • (1993) Acta Crystallogr. D Biol. Crystallogr , vol.49 , pp. 234-245
    • Madhusudan1    Kodandapani, R.2    Vijayan, M.3
  • 76
    • 80955133161 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex
    • Andres, S.N.; Junop, M.S. Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2011, 67, 1399-1402.
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.67 , pp. 1399-1402
    • Andres, S.N.1    Junop, M.S.2
  • 78
    • 27744598146 scopus 로고    scopus 로고
    • Purification, crystallization, and properties of F1-ATPase complexes from the thermoalkaliphilic Bacillus sp. strain TA2.A1
    • Stocker, A.; Keis, S.; Cook, G.M.; Dimroth, P. Purification, crystallization, and properties of F1-ATPase complexes from the thermoalkaliphilic Bacillus sp. strain TA2.A1. J. Struct. Biol. 2005, 152, 140-145.
    • (2005) J. Struct. Biol , vol.152 , pp. 140-145
    • Stocker, A.1    Keis, S.2    Cook, G.M.3    Dimroth, P.4
  • 79
    • 0001654293 scopus 로고
    • Crystal growth and crystal improvement strategies
    • Schick, B.; Jurnak, F. Crystal growth and crystal improvement strategies. Acta Crystallogr. F 1994, 50, 563-568.
    • (1994) Acta Crystallogr. F , vol.50 , pp. 563-568
    • Schick, B.1    Jurnak, F.2
  • 80
    • 0343907251 scopus 로고    scopus 로고
    • Engineering of diffraction-quality crystals of the NF-kappaB P52 homodimer:DNA complex
    • Cramer, P.; Muller, C.W. Engineering of diffraction-quality crystals of the NF-kappaB P52 homodimer:DNA complex. FEBS Lett. 1997, 405, 373-377.
    • (1997) FEBS Lett , vol.405 , pp. 373-377
    • Cramer, P.1    Muller, C.W.2
  • 81
    • 78650123497 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of a calcineurin B-like protein 1 (CBL1) mutant from Ammopiptanthus mongolicus
    • Shang, G.; Cang, H.; Liu, Z.; Gao, W.; Bi, R. Crystallization and preliminary crystallographic analysis of a calcineurin B-like protein 1 (CBL1) mutant from Ammopiptanthus mongolicus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2010, 66, 1602-1605.
    • (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.66 , pp. 1602-1605
    • Shang, G.1    Cang, H.2    Liu, Z.3    Gao, W.4    Bi, R.5
  • 82
    • 68349137531 scopus 로고    scopus 로고
    • A description of the structural determination procedures of a gap junction channel at 3.5 A resolution
    • Suga, M.; Maeda, S.; Nakagawa, S.; Yamashita, E.; Tsukihara, T. A description of the structural determination procedures of a gap junction channel at 3.5 A resolution. Acta Crystallogr. D Biol. Crystallogr. 2009, 65, 758-766.
    • (2009) Acta Crystallogr. D Biol. Crystallogr , vol.65 , pp. 758-766
    • Suga, M.1    Maeda, S.2    Nakagawa, S.3    Yamashita, E.4    Tsukihara, T.5
  • 84
    • 40449127948 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC
    • Ravaud, S.; Wild, K.; Sinning, I. Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2008, 64, 144-148.
    • (2008) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.64 , pp. 144-148
    • Ravaud, S.1    Wild, K.2    Sinning, I.3
  • 86
    • 0034503345 scopus 로고    scopus 로고
    • A novel free-mounting system for protein crystals: Transformation and improvement of diffraction power by accurately controlled humidity changes
    • Kiefersauer, R.; Than, M.E.; Dobbek, H.; Gremer, L.; Melero, M.; Strobl, S.; Dias, J.M.; Soulimane, T.; Huber, R. A novel free-mounting system for protein crystals: transformation and improvement of diffraction power by accurately controlled humidity changes. J. Appl. Cryst. 2000, 33, 1223-1230.
    • (2000) J. Appl. Cryst , vol.33 , pp. 1223-1230
    • Kiefersauer, R.1    Than, M.E.2    Dobbek, H.3    Gremer, L.4    Melero, M.5    Strobl, S.6    Dias, J.M.7    Soulimane, T.8    Huber, R.9
  • 88
    • 0036101649 scopus 로고    scopus 로고
    • Protein crystallography in a vapour stream: Data collection, reaction initiation and intermediate trapping in naked hydrated protein crystals
    • Sjogren, T.; Carlsson, G.; Larsson, G.; Hajdu, A.; Andersson, C.; Pettersson, H.; Hajdu, J. Protein crystallography in a vapour stream: Data collection, reaction initiation and intermediate trapping in naked hydrated protein crystals. J. Appl. Cryst. 2002, 35, 113-116.
    • (2002) J. Appl. Cryst , vol.35 , pp. 113-116
    • Sjogren, T.1    Carlsson, G.2    Larsson, G.3    Hajdu, A.4    Andersson, C.5    Pettersson, H.6    Hajdu, J.7
  • 89
    • 84855991023 scopus 로고    scopus 로고
    • Measurement of the equilibrium relative humidity for common precipitant concentrations: Facilitating controlled dehydration experiments
    • Wheeler, M.J.; Russi, S.; Bowler, M.G.; Bowler, M.W. Measurement of the equilibrium relative humidity for common precipitant concentrations: Facilitating controlled dehydration experiments. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2012, 68, 111-114.
    • (2012) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.68 , pp. 111-114
    • Wheeler, M.J.1    Russi, S.2    Bowler, M.G.3    Bowler, M.W.4
  • 90
    • 0032166395 scopus 로고    scopus 로고
    • Densities of poly(ethylene glycol) + water mixtures in the 298.15-328.15 K temperature range
    • Eliassi, A.; Modarress, H. Densities of poly(ethylene glycol) + water mixtures in the 298.15-328.15 K temperature range. J. Chem. Eng. Data 1998, 43, 719-772.
    • (1998) J. Chem. Eng. Data , vol.43 , pp. 719-772
    • Eliassi, A.1    Modarress, H.2
  • 91
    • 77950828673 scopus 로고    scopus 로고
    • Progress in rational methods of cryoprotection in macromolecular crystallography
    • Alcorn, T.; Juers, D.H. Progress in rational methods of cryoprotection in macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 2010, 66, 366-373.
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 366-373
    • Alcorn, T.1    Juers, D.H.2
  • 92
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 1968, 33, 491-497. 93.
    • (1968) J. Mol. Biol , vol.33 , Issue.491-497 , pp. 93
    • Matthews, B.W.1
  • 93
    • 33751288470 scopus 로고    scopus 로고
    • Synthesis and interaction with human serum albumin of the first 3,18-disubstituted derivative of bilirubin
    • Painter, L.; Harding, M.M.; Beeby, P.J. Synthesis and interaction with human serum albumin of the first 3,18-disubstituted derivative of bilirubin. J. Chem. Soc. Perkin Trans. 1998, 18, 3041-3050.
    • (1998) J. Chem. Soc. Perkin Trans , vol.18 , pp. 3041-3050
    • Painter, L.1    Harding, M.M.2    Beeby, P.J.3
  • 94
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsky, Z.; Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowsky, Z.1    Minor, W.2
  • 96
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 A resolution
    • Sugio, S.; Kashima, A.; Mochizuki, S.; Noda, M.; Kobayashi, K. Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999, 12, 439-446.
    • (1999) Protein Eng , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.