Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station.: 2.: Comparison of crystal quality by X-ray diffraction

被引:11
作者
Berisio, R
Vitagliano, L
Vergara, A
Sorrentino, G
Mazzarella, L
Zagari, A
机构
[1] CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy
[2] Univ Naples Federico II, Dipartimento Chim, I-80126 Naples, Italy
[3] Univ Naples Federico II, Dipartimento Chim Biol, Sez Biostrutture, I-80134 Naples, Italy
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷
关键词
collagen; triple helix; ISS; microgravity; APCF; X-ray diffraction;
D O I
10.1107/S0907444902014427
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Crystals of the collagen-like polypeptide (PPG)(10) were obtained within the Advanced Protein Crystallization Facility on board the International Space Station, during the STS-105/STS-108 mission. The duration of this mission was such to ensure that the crystallization process had reached its end. Crystals were grown both in the presence and in the absence of agarose gel, to compare the quality of the crystals obtained from these different environments. As a result, crystals grown in the absence of agarose on Earth as well as in microgravity showed X-ray diffraction up to 1.15 Angstrom. The intensity/sigma ratio was slightly higher for microgravity grown crystals. Crystals grown in agarose gel, both in microgravity and on ground, showed a comparable diffraction power, with a resolution limit of 1.45 Angstrom.
引用
收藏
页码:1695 / 1699
页数:5
相关论文
共 27 条
[1]   Recent progress on collagen triple helix structure, stability and assembly [J].
Berisio, R ;
Vitagliano, L ;
Mazzarella, L ;
Zagari, A .
PROTEIN AND PEPTIDE LETTERS, 2002, 9 (02) :107-116
[2]   Effects of microgravity on the crystal quality of a collagen-like polypeptide [J].
Berisio, R ;
Vitagliano, L ;
Sorrentino, G ;
Carotenuto, L ;
Piccolo, C ;
Mazzarella, L ;
Zagari, A .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2000, 56 :55-61
[3]   Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 [J].
Berisio, R ;
Vitagliano, L ;
Mazzarella, L ;
Zagari, A .
PROTEIN SCIENCE, 2002, 11 (02) :262-270
[4]   EXPERIMENT EQUIPMENT FOR PROTEIN CRYSTALLIZATION IN MU-G FACILITIES [J].
BOSCH, R ;
LAUTENSCHLAGER, P ;
POTTHAST, L ;
STAPELMANN, J .
JOURNAL OF CRYSTAL GROWTH, 1992, 122 (1-4) :310-316
[5]   1.7 Å X-ray structure of space-grown collagenase crystals [J].
Broutin-L'Hermite, I ;
Ries-Kautt, M ;
Ducruix, A .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2000, 56 :376-378
[6]   Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 [J].
Carotenuto, L ;
Berisio, R ;
Piccolo, C ;
Vitagliano, L ;
Zagari, A .
JOURNAL OF CRYSTAL GROWTH, 2001, 232 (1-4) :481-488
[7]   Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 Å resolution [J].
Dong, J ;
Boggon, TJ ;
Chayen, NE ;
Raftery, J ;
Bi, RC ;
Helliwell, JR .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1999, 55 :745-752
[8]   A hyperstable collagen mimic [J].
Holmgren, SK ;
Bretscher, LE ;
Taylor, KM ;
Raines, RT .
CHEMISTRY & BIOLOGY, 1999, 6 (02) :63-70
[9]   Insights on the conformational stability of collagen [J].
Jenkins, CL ;
Raines, RT .
NATURAL PRODUCT REPORTS, 2002, 19 (01) :49-59
[10]   X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) [J].
Kramer, RZ ;
Vitagliano, L ;
Bella, J ;
Berisio, R ;
Mazzarella, L ;
Brodsky, B ;
Zagari, A ;
Berman, HM .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 280 (04) :623-638