The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Application Status
This application is a US Non-provisional patent application filed on 04/07/2023.
Claims 1-16, 17, 74, 85, 88, 93, 96-98, and 133 are currently pending in the instant patent application.
The preliminary amendment filed on 09/07/2023, amending claims 3, 5, 8-10, 12, 14, 17, 74, 85, 88, 93, 96-98, and 133, and canceling claims 18-73, 75-84, 86-87, 59-92, 94-95, 99-132, and 134-158 is acknowledged.
Election/Restriction
Applicant's election without traverse of Group I, Claims 1-16, drawn to an orthogonal tRNA synthetase (O-RS) comprising a substitution of at least one of the following residues as compared to a wild-type M. janneschii tRNA synthetase (SEQ ID NO:45): (a) T11, (b) I15, (c) D27, (d) M96, (e) G97, and (f) K101 in the response filed on 01/05/2026 is acknowledged.
Claims 17, 74, 85, 88, 93, 96-98, and 133 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Applicants request for rejoinder is noted. However, current claims of elected Group I are not allowable at this time. When Group I would be allowable, rejoinder request would be evaluated at that time.
The requirement is still deemed proper and is therefore made FINAL.
Claims 1-16 are present for examination.
Priority
Acknowledgement is made of applicants claim for priority of US Provisional application 63/328,854, filed on 04/18/2022.
Information Disclosure Statement
There is no information disclosure statement (IDS) with this patent application.
Specification Objections
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code (see, pg 16). See MPEP § 608.01.
Drawings
Drawings submitted on 09/07/2023 are accepted by the Examiner.
Claims objections
Claim 1 is objected to in the recitation “M. janneschii”; as abbreviations should not be used without at least once fully setting forth what they are used for. Appropriate correction is required.
Claim 3 is objected to in the recitation “O-RS comprises at least one of the following substitutions”, which should be changed to “O-RS comprises at least one of the following (a) to (f) substitutions”. Appropriate correction is required.
Claim 6 is objected to in the recitation “O-RS comprises at least one of the following substitutions”, which should be changed to “O-RS comprises at least one of the following (a) to (f) substitutions”. Appropriate correction is required.
Claims 15 and 16 are objected to in the recitation “selected from SEQ ID NOs: 39-44 and 46-56”; which should be changed to “selected from the group consisting of SEQ ID NOs: 39-44 and 46-56”. Appropriate correction is required.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless -
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
MPEP-2131 Anticipation — Application of 35 U.S.C. 102 [R-08.2017]
A claimed invention may be rejected under 35 U.S.C. 102 when the invention is anticipated (or is "not novel") over a disclosure that is available as prior art. To reject a claim as anticipated by a reference, the disclosure must teach every element required by the claim under its broadest reasonable interpretation. See, e.g., MPEP § 2114, subsections II and IV.
"A claim is anticipated only if each and every element as set forth in the claim is found, either expressly or inherently described, in a single prior art reference." Verdegaal Bros. v. Union Oil Co. of California, 814 F.2d 628, 631, 2 USPQ2d 1051, 1053 (Fed. Cir. 1987). "When a claim covers several structures or compositions, either generically or as alternatives, the claim is deemed anticipated if any of the structures or compositions within the scope of the claim is known in the prior art." Brown v. 3M, 265 F.3d 1349, 1351, 60 USPQ2d 1375, 1376 (Fed. Cir. 2001) Note that, in some circumstances, it is permissible to use multiple references in a 35 U.S.C. 102 rejection. See MPEP § 2131.01.
MPEP-2131.01 Multiple Reference 35 U.S.C. 102 Rejections [R-11.2013]
Normally, only one reference should be used in making a rejection under 35 U.S.C. 102. However, a 35 U.S.C. 102 rejection over multiple references has been held to be proper when the extra references are cited to:
(A) Prove the primary reference contains an "enabled disclosure;"
(B) Explain the meaning of a term used in the primary reference; or
(C) Show that a characteristic not disclosed in the reference is inherent.
Claims 1-7, and 14-15 are rejected under 35 U.S.C. 102(a)(1) based upon a public use or sale or other public availability of the invention as anticipated by UniProt Accession Number A0A076LH95; Created 10/29/2014; Title- Tyrosyl-tRNA synthetase derived from Methanocaldococcus bathoardescens sp.).
The Broadest Reasonable Interpretation (BRI) of claims 1-2, which is drawn to an orthogonal tRNA synthetase (O-RS) comprising a substitution of at least one of the following residues as compared to a wild-type M. janneschii tRNA synthetase (SEQ ID NO:45): (a) T11, (b) I15, (c) D27, (d) M96, (e) G97, and (f) K101, wherein the M. janneschii tRNA synthetase is at least 85% identical to SEQ ID NO: 45.
Regarding claims 1-7, and 14-15, UniProt Accession Number A0A076LH95 teaches a tyrosyl tRNA synthetase (O-RS) gene encoding protein from Methanocaldococcus bathoardescens sp., an Archaea and a methane-bacteria, which is 93.6% identity compared to wild-type M. janneschii tRNA synthetase of SEQ ID NO: 45, and 93.2% identical to SEQ ID NO: 39 of the instant application (see, sequence alignments as shown below), inherently an orthogonal tRNA synthetase, wherein said O-RS comprises a mutation at position I15 corresponding to SEQ ID NO: 45 is I15V, and further comprises mutations D2N, M6I, R21K, G158D,
Because the tyrosyl tRNA synthetase (O-RS) gene encoding protein from Methanocaldococcus bathoardescens sp., an Archaea and a methane-bacteria, which is 93.6% identity to wild-type M. janneschii tRNA synthetase of SEQ ID NO: 45 as claimed and of the reference is one and the same, Examiner takes the position that said tRNA synthetase of reference is inherently an orthogonal tRNA synthetase. Since the Office does not have the facilities for examining and comparing applicants' enzyme and the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed product enzyme and the product (enzyme) of the prior art. See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594.
RESULT 2
A0A076LH95_9EURY
ID A0A076LH95_9EURY Unreviewed; 306 AA.
AC A0A076LH95;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-OCT-2025, entry version 48.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02008};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02008};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02008};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02008};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02008};
GN ORFNames=JH146_1435 {ECO:0000313|EMBL:AIJ06277.1};
OS Methanocaldococcus bathoardescens.
RX PubMed=25634941; DOI=10.1099/ijs.0.000097;
RA Stewart L.C., Jung J.H., Kim Y.T., Kwon S.W., Park C.S., Holden J.F.;
RT "M ethanocaldococcus bathoardescens sp. nov., a hyperthermophilic
RT methanogen isolated from a volcanically active deep-sea hydrothermal
RT vent.";
RL Int. J. Syst. Evol. Microbiol. 65:1280-1283(2015).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000256|HAMAP-
CC Rule:MF_02008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Tyr) + L-tyrosine + ATP = L-tyrosyl-tRNA(Tyr) + AMP +
CC diphosphate + H(+); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00048248, ECO:0000256|HAMAP-
CC Rule:MF_02008};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_02008}.
FT MOTIF 37..45
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT MOTIF 204..208
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 32
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 151
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 155
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 158
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 173
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
SQ SEQUENCE 306 AA; 35100 MW; EE2A5C013AA59A1E CRC64;
Query Match 93.6%; Score 1464; Length 306;
Best Local Similarity 93.1%;
Matches 285; Conservative 13; Mismatches 8; Indels 0; Gaps 0;
Qy 1 MDEFEMIKRNTSEIISEEELREVLKKDEKSAVIGFEPSGKIHLGHYLQIKKMIDLQNAGF 60
|:|||:||||||||:|||||:|||||||||| ||||||||||||||||||||||||||||
Db 1 MNEFEIIKRNTSEIVSEEELKEVLKKDEKSAYIGFEPSGKIHLGHYLQIKKMIDLQNAGF 60
Qy 61 DIIIYLADLHAYLNQKGELDEIRKIGDYNKKVFEAMGLKAKYVYGSEHGLDKDYTLNVYR 120
|||| ||||||||||||||||||:||:|||:|||||||||||||||| ||||||||||:
Db 61 DIIILLADLHAYLNQKGELDEIREIGEYNKRVFEAMGLKAKYVYGSEFQLDKDYTLNVYK 120
Qy 121 LALKTTLKRARRSMELIAREDENPKVAEVIYPIMQVNGIHYEGVDVAVGGMEQRKIHMLA 180
||||||||||||||||||||||||||||||||||||| |:| |||||||||||||||||
Db 121 LALKTTLKRARRSMELIAREDENPKVAEVIYPIMQVNDIYYLDVDVAVGGMEQRKIHMLA 180
Qy 181 RELLPKKVVCIHNPVLTGLDGEGKMSSSKGNFIAVDDSPEEIRAKIKKAYCPAGVVEGNP 240
|||||||||||||||||||||||||||||||||||||||||||||||||||||||:||||
Db 181 RELLPKKVVCIHNPVLTGLDGEGKMSSSKGNFIAVDDSPEEIRAKIKKAYCPAGVIEGNP 240
Qy 241 IMEIAKYFLEYPLTIKRPEKFGGDLTVNSYEELESLFKNKELHPMDLKNAVAEELIKILE 300
||||||||||||||| ||||||||||||:|||||:|||||||||||||||||||||||||
Db 241 IMEIAKYFLEYPLTINRPEKFGGDLTVNNYEELETLFKNKELHPMDLKNAVAEELIKILE 300
Qy 301 PIRKRL 306
||||:|
Db 301 PIRKKL 306
Therefore, UniProt Accession Number A0A076LH95 anticipates claims 1-7, and 14-15 of the instant application as written.
Claims 1, 3-6 and 7 are rejected under 35 U.S.C. 102(a)(1) based upon a public use or sale or other public availability of the invention as anticipated by UniProt Accession Number K2RRN6; Created 11/28/2012; Title- Tyrosyl-tRNA synthetase derived from Methanocaldococcus bathoardescens sp.).
The Broadest Reasonable Interpretation (BRI) of claims 1, which is drawn to an orthogonal tRNA synthetase (O-RS) comprising a substitution of at least one of the following residues as compared to a wild-type M. janneschii tRNA synthetase (SEQ ID NO:45): (a) T11, (b) I15, (c) D27, (d) M96, (e) G97, and (f) K101.
Regarding claims 1, 3-6 and 7, UniProt Accession Number A0A076LH95 teaches a tyrosyl tRNA synthetase (O-RS) gene encoding protein from Methanobacterium formicicum, an Archaea and a methane-bacteria, which is 57.1% identity compared to wild-type M. janneschii tRNA synthetase of SEQ ID NO: 45 of the instant application (see, sequence alignments as shown below), inherently an orthogonal tRNA synthetase, wherein said O-RS comprises mutations at position T11, I15 corresponding to SEQ ID NO: 45 are T11A, I15V, M96L, K101E, and further comprises mutations R21K, G158D, and M285L,
Because the tyrosyl tRNA synthetase (O-RS) gene encoding protein from Methanocaldococcus bathoardescens sp., an Archaea and a methane-bacteria, which is 93.6% identity to wild-type M. janneschii tRNA synthetase of SEQ ID NO: 45 as claimed and of the reference is one and the same, Examiner takes the position that said tRNA synthetase of reference is inherently an orthogonal tRNA synthetase. Since the Office does not have the facilities for examining and comparing applicants' enzyme and the prior art, the burden is on the applicant to show a novel or unobvious difference between the claimed product enzyme and the product (enzyme) of the prior art. See In re Best, 562 F.2d 1252, 195 USPQ 430 (CCPA 1977) and In re Fitzgerald et al., 205 USPQ 594.
RESULT 42
K2RRN6_METFP
ID K2RRN6_METFP Unreviewed; 320 AA.
AC K2RRN6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 08-OCT-2025, entry version 51.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02008};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02008};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02008};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02008};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02008};
GN ORFNames=A994_08151 {ECO:0000313|EMBL:EKF85390.1};
OS Methanobacterium formicicum (strain DSM 3637 / PP1).
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1204725 {ECO:0000313|EMBL:EKF85390.1, ECO:0000313|Proteomes:UP000007360};
RN [1] {ECO:0000313|EMBL:EKF85390.1, ECO:0000313|Proteomes:UP000007360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3637 / PP1 {ECO:0000313|Proteomes:UP000007360};
RX PubMed=23209223; DOI=10.1128/JB.01829-12;
RA Gutierrez G.;
RT "Draft genome sequence of Methanobacterium formicicum DSM 3637, an
RT archaebacterium isolated from the methane producer amoeba Pelomyxa
RT palustris.";
RL J. Bacteriol. 194:6967-6968(2012).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000256|HAMAP-
CC Rule:MF_02008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Tyr) + L-tyrosine + ATP = L-tyrosyl-tRNA(Tyr) + AMP +
CC diphosphate + H(+); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00048248, ECO:0000256|HAMAP-
CC Rule:MF_02008};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_02008}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
FT MOTIF 40..48
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT MOTIF 213..217
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 35
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 156
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 160
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 163
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 178
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02008"
SQ SEQUENCE 320 AA; 35841 MW; 0947EC0C599AA91F CRC64;
Query Match 57.1%; Score 893; Length 320;
Best Local Similarity 58.2%;
Matches 178; Conservative 54; Mismatches 64; Indels 10; Gaps 4;
Qy 7 IKRNTSEIISEEELREVLKKDEKSAVIGFEPSGKIHLGHYLQIKKMIDLQNAGFDIIIYL 66
|:: |::: |||:| |:|| |:| ||:|||||:|||| : :||||||| ||| | | |
Db 10 IEQGALEVVTPEELKEKLEKDPKTAYIGYEPSGKVHLGHAITVKKMIDLQKAGFKIKILL 69
Qy 67 ADLHAYLNQKGELDEIRKIGDYNKKVFEAMGLK--AKYVYGSEHGLDKDYTLNVYRLALK 124
|||||||| || |:||::| :|||: | |:|| ::: || ::|||: ||:||:
Db 70 ADLHAYLNGKGSLEEIKEISEYNKQCFRALGLSEDTEFILGSSFQTEEDYTMKVYQLAIS 129
Qy 125 TTLKRARRSMELIAREDENPKVAEVIYPIMQVNGIHYEGVDVAVGGMEQRKIHMLARELL 184
||| |||||| |:|: |: :|||||||:||| : : |||:|||||||||||||||: |
Db 130 TTLTRARRSMAQISRDAEDHQVAEVIYPLMQVVDMLFLGVDLAVGGMEQRKIHMLARDNL 189
Qy 185 PK----KVVCIHNPVLTGLDGEGKMSSSKGNFIAVDDSPEEIRAKIKKAYCPAGVVEGNP 240
|| |||| |:| | || |||||| ||||:|| || | ||||:||||| |||||
Db 190 PKLGFQSPVCIHTPLLHGTDGSDKMSSSKENFIAIDDEPEVINKKIKKSYCPAGEVEGNP 249
Qy 241 IMEIAKYFL---EYPLTIKRPEKFGGDLTVNSYEELESLFKNKELHPMDLKNAVAEELIK 297
::||| :|: : | | ||:||||:| : : ||| :: : :|||:|||| ||| | :
Db 250 VLEIAHHFIFSEKDTLLITRPDKFGGNLEL-TQEELIQMYGDGKLHPLDLKNGVAESLTE 308
Qy 298 ILEPIR 303
||||:|
Db 309 ILEPVR 314
Therefore, UniProt Accession Number UniProt Accession Number K2RRN6 anticipates claims 1, 3-6 and 7 of the instant application as written.
Conclusion
Status of the claims:
Allowable Subject Matter
Claims 8-13 and 16 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Claims 1-7, 14 and 15 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to IQBAL H CHOWDHURY whose telephone number is (571)272-8137. The examiner can normally be reached on M-F, at 9:00-5:00 PM.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
Iqbal H. Chowdhury, Primary Patent Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office (USPTO)
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656
Prosecution Insights