Crystallization of the collagen-like polypeptide (PPG)(10) aboard the International Space Station. 1. Video observation
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Crystallization of the collagen-like polypeptide (PPG)(10) aboard the International Space Station. 1. Video observation (115 visite)

Vergara A, Corvino E, Sorrentino G, Piccolo C, Tortora A, Carotenuto L, Mazzarella L, Zagari A

Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58: 1690-1694.



Tipo di articolo: Journal Article,

Impact factor: 1.76, Impact factor a 5 anni: 9.416

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036793496&partnerID=40&md5=e79d94d9e72c7924fcd5976441fb7b47

Parole chiave: Advanced Protein Crystallization Facility, Crystallogenesis, Microgravity, (prolyl Prolyl Glycine)10, (prolyl-Prolyl-Glycine)10, Collagen, Peptide, Sepharose, Chemistry, Comparative Study, Conference Paper, Flight Experiment, Iss Project, Long Duration, Manned, Methodology, Solution And Solubility, Space Flight, Videorecording, Weightlessness, Time Factors, Video Recording, (prolyl Prolyl Glycine) 10, (prolyl-Prolyl-Glycine) 10,

Affiliazioni:

*** IBB - CNR ***
Dipartimento di Chimica Biologica, Universita degli Studi di Napoli, Via Mezzocannone 6, Napoli, Italy


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Single chains of the collagen model polypeptide with sequence (Pro-Pro-Gly)(10), hereafter referred to as (PPG)(10), aggregate to form rod-shaped triple helices. Crystals of (PPG)(10) were grown in the Advanced Protein Crystallization Facility (APCF) both onboard the International Space Station (ISS) and on Earth. The experiments allow the direct comparison of four different crystallization environments for the first time: solution in microgravity (mug), agarose gel in mug, solution on earth, and gel on earth. Both on board and on ground, the crystal growth was monitored by a CCD video camera. The image analysis provided information on the spatial distribution of the crystals, their movement and their growth rate. The analysis of the distribution of crystals reveals that the crystallization process occurs as it does in batch conditions. Slow motions have been observed onboard the ISS. Different to Space-Shuttle experiment, the crystals onboard the ISS moved coherently and followed parallel trajectories. Growth rate and induction time are very similar both in gel and in solution, suggesting that the crystal growth rate is controlled by the kinetics at the interface under the used experimental conditions. These results provide the first data in the crystallogenesis of (PPG)(10), which is a representative member of non-globular, rod-like proteins.
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Impact Factor: 1.76
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Improta R, Mele F, Crescenzi O, Benzi C, Barone V
* Understanding the role of stereoelectronic effects in determining collagen stability. 2. A quantum mechanical/molecular mechanical study of (Proline-Proline-Glycine)n polypeptides (128 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Jul 3; 124(26): 7857-7865.
Impact Factor: 6.201
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Recent progress on collagen triple helix structure, stability and assembly (99 visite)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 107-116.
Impact Factor: 0.622
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (100 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
Impact Factor: 3.546
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Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A
* Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability (112 visite)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
Impact Factor: 3.472
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Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Structural bases of collagen stabilization induced by proline hydroxylation (105 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001 Apr 15; 58(5): 459-464.
Impact Factor: 1.845
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Carotenuto L, Cartwright J, Otálora F, Garcia-ruiz J, Castagnolo D, Piccolo C, Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Depletion Zone Around Sedimenting Protein Crystals In Microgravity (86 visite)
Esa Journal, 2001; 454: 323-329.
Impact Factor: 0.895
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Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Erratum: Structural bases of collagen stabilization induced by proline Hydroxylation (Biopolymers (2001) 58: 5 (459-464)) (134 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001; 59(6): 465-465.
Impact Factor: 1.845
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (91 visite)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
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Berisio R, Vitagliano L, Sorrentino G, Carotenuto L, Piccolo C, Mazzarella L, Zagari A
Effects of microgravity on the crystal quality of a collagen-like polypeptide (96 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2000 Jan; 56(1): 55-61.
Impact Factor: 3.067
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Carotenuto L, Castagnolo D, Piccolo C, Berisio R, Vitagliano L, Mazzarella L, Zagari A
Biomolecule crystallisation in microgravity (76 visite)
Eur Space Agency Spec Publ Esa Sp (ISSN: 0379-6566), 2000; (454I): 437-443.
Impact Factor: 3.445
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (107 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
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Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (114 visite)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1998 Jul 24; 280(4): 623-638.
Impact Factor: 5.803
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 Esposito L, Sica F, Sorrentino G, Berisio R, Carotenuto L, Giordano A, Raia C, Rossi M, Lamzin VS, Willson KS, Zagari A
Protein Crystal Growth In The Advance Protein Crystallisation Facility On The Lms Mission: A Comparison Of Sulfolobus Solfataricus Alchool Dehydrogenase Crystals Grown On The Ground And In Microgravity (75 visite)
Acta Crystallogr D Biol Crystallogr, 1998; 54: 386-390.
Impact Factor: 0
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Esposito L, Sica F, Sorrentino G, Berisio R, Carotenuto L, Giordano A, Raia CA, Rossi M, Lamzin VS, Wilson KS, Zagari A
Protein crystal growth in the advanced protein crystallization facility on the LMS mission: A comparison of Sulfolobus solfataricus alcohol dehydrogenase crystals grown on the ground and in microgravity (102 visite)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 1998; 54(3): 386-390.
Impact Factor: 2.244
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Oliva A, Marrone G, Della Ragione F, Riccio V, Palumbo R, Rossano F, Zappia V
Isolation and characterization of human embryonic osteoblasts (81 visite)
Calcif Tissue Int (ISSN: 0171-967xprint, 0171-967xlinking), 1992 Nov; 51(5): 356-362.
Impact Factor: 2.364
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52 Records (48 escludendo Abstract e Conferenze).
Impact factor totale: 166.286 (146.473 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 212.951 (191.787 escludendo Abstract e Conferenze).







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